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(2R)-2-amino-4-benzylpentanedioic acid
-
-
(2R,4R)-2-amino-4-(2-benzo[b]furyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-benzo[b]thiazolyl)methyl pentanedioic acid
-
IC50: 0.38 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-benzo[b]thienyl)methyl pentanedioic acid
-
IC50: 0.036 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-indolyl)methyl pentanedioic acid
-
IC50: 9.8 mg/l, minimum inhibitor concentration: 62.5 mg/l
(2R,4R)-2-amino-4-(2-thienyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: above 1.0 mg/l
(2R,4R)-2-amino-4-[(3-chloro)-2-benzo[b]thienyl]methyl pentanedioic acid
-
IC50: 0.01 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(2-bromo)benzyl pentanedioic acid
-
IC50: 6.3 mg/l, minimum inhibitor concentration: 31.3 mg/l
(2R,4S)-2-amino-4-(2-chloro)benzyl pentanedioic acid
-
IC50: 7.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
(2R,4S)-2-amino-4-(3,4,5-trimethoxy)benzyl pentanedioic acid
-
IC50: 81 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-(3,5-dichloro)benzyl pentanedioic acid
-
IC50: 3.0 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-benzo[b]thienyl)methyl pentanedioic acid
-
IC50: 1.7 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(3-bromo)benzyl pentanedioic acid
-
IC50: 0.13 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-chloro)benzyl pentanedioic acid
-
IC50: 3.4 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(3-cyclohexyl)propyl pentanedioic acid
-
IC50: 0.6 mg/l, MIC: 2.0 mg/l
(2R,4S)-2-amino-4-(3-methoxy)benzyl pentanedioic acid
-
IC50: 0.2 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)benzyl pentanedioic acid
-
IC50: 0.7 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propargyl pentanedioic acid
-
IC50: 0.37 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-chloro)benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-methoxy)benzyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(4-phenyl)benzyl pentanedioic acid
-
IC50: 0.078 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-tert-butyl)benzyl pentanedioic acid
-
IC50: 0.6 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(5-phenyl-2E,4E-pentadienyl)pentanedioic acid
-
IC50: 9.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(prop-2-ynyl) pentanedioic acid
-
IC50: 5.5 mg/l, MIC: 31.3 mg/l
(2R,4S)-2-amino-4-[3-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-[3-(2-furyl)]benzyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.65 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-[4-(2-naphthyl)]benzyl pentanedioic acid
-
IC50: 0.42 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-[4-(3-thienyl)]benzyl pentanedioic acid
-
IC50: 0.32 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(n-benzenesulfonylamino)]benzyl pentanedioic acid
-
IC50: 10.2 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-[4-(N-phenylaminocarbonyl)amino]-benzyl pentanedioic acid
-
IC50: 0.49 mg/l, minimum inhibitor concentration: 15.6 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl) pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.4 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(2R,4S,E)-2-amino-4-[3-(2-naphthyl)prop-2-enyl]pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4R)-2-amino-4-benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4S)-2-amino-4-(1-naphthyl)methyl pentanedioic acid
-
IC50: 5.6 mg/l, minimum inhibitor concentration: 3.9 mg/l
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(R,S)-1-hydroxy-1-oxo-4-amino-4-carboxyphosphorinane
-
-
(R,S)-4-amino-4-carboxy-1,1-dioxotetrahydro-thiopyran
-
-
1,1-dioxo-tetrahydrothiopyran-4-one
-
-
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
-
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
-
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
-
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylurea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)thiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)urea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)thiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)urea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-methoxyphenyl)urea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)urea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)urea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylthiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylurea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-isopropylurea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
-
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylurea
-
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Binding pose and the interaction pattern of the compound, non-competitive inhibition
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
-
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
1-(4-methoxyphenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
1-benzyl-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
-
1-hydroxyphosphinan-4-one 1-oxide
-
-
1H-benzimidazole-2-sulfonic acid
-
-
2-(2-Carboxyethyl)aziridine-2-carboxylic acid
-
i.e. aziridino-glutamate, inactivates glutamate racemase by alkylating an active site Cys residue
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
2-amino-4-phosphonobutanoic acid
-
-
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
2-hydroxy-3,4,5-trioxocyclopent-1-en-1-olate
-
-
2-nitro-5-thiocyanatobenzoate
0.2 mM
2-Nitro-5-thiocyanobenzoate
2-[(5-chloro-1-methyl-1H-indol-3-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
analysis of mouse and human internal clearance
2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-7-(2-methylpropyl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-3-(1-methyl-1H-pyrrol-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(pent-4-yn-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-en-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-yn-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(propan-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(3-hydroxyprop-2-yn-1-yl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-1,2,4-triazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-pyrazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-4H-1,2,4-triazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
2-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
3-(2-amino-4-methyl-1,3-thiazol-5-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
3-(2-amino-5-methyl-1,3-thiazol-4-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
3-(4-acetyl-1-methyl-1H-pyrrol-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
3-(5-methylbenzo[d]oxazol-2-yl)aniline
-
-
3-(benzo[d]oxazol-2-yl)aniline
-
-
3-sulfobenzoic acid
structural analogue of dipicolinate dianion
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
4-chlorobenzene-1,2,3-triol
-
noncompetitive inhibition
4-hydroxybenzene-1,3-disulfonate
-
-
4-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-5-methylfuran-2-carbonitrile
-
-
5,5'-dithiobis(2-nitrobenzoate)
5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-(pyridin-4-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
5-[2-[(6-chloro-1,2-dihydroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 1 and 0.5 microg/ml
5-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-(cyanomethyl)-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(propan-2-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-1,2,3-triazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-pyrazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-1,2,4-triazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-pyrazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(2-hydroxyethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(4-hydroxybut-2-yn-1-yl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-4-methylfuran-2-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(1H-imidazol-1-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-[5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl]-1H-pyrrole-3-sulfonamide
analysis of mouse and human internal clearance
5-[5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[5-(but-3-yn-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[7-(cyclopropylmethyl)-5-methyl-2-[(5-methyl-1H-indol-3-yl)methyl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-N-methoxy-1-methyl-1H-pyrrole-3-carboxamide
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 16 microg/ml
6-chloro-4-([7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfinyl)-1H-pyrrol-2-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl]methyl)isoquinoline-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 16 and 8 microg/ml
6-chloro-4-[[3-(4-cyano-1-methyl-1H-pyrrol-2-yl)-7-(cyclopropylmethyl)-4,6-dioxo-5-prop-2-yn-1-yl-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl]methyl]isoquinoline-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 2 and 1 microg/ml
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
benzene-1,3-disulfonate
-
-
beta-chloro-L-alanine
BCLA, modifies BsMurI predominantly at C74, the cysteine residue responsible for deprotonation of an incoming D-Glu substrate
bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex
-
binding structure, overview
-
bis(2-carboxyethyl)-phosphinic acid
-
-
Cu2+
-
inhibition is completely reversed by EDTA
D-glutamate
-
MurI of Helicobacter pylori is strongly inhibited by D-glutamate
D-N-Hydroxyglutamate
-
the compound acts as alternate substrate and is converted into 2-oxoglutarate and NH4+. Km: 0.057 mM, turnover number: 1080 min-1. An imine intermediate is likely the species causing the inhibition
exiguaquinol
-
pentacyclic hydroquinone from Neopetrosia exigua, protein-ligand modeling
gamma-2-naphthylmethyl-D-glutamate
potent competitive inhibitor that induces a disorder in one of the loops near the active site
L-alpha-aminohexanedioate
-
-
L-N-Hydroxyglutamate
-
weak
L-serine-O-sulfate
-
suicide substrate. The glutamate racemase catalyzes alpha,beta-elimination of L-serine O-sulfate to produce a pyruvate concomitantly with an irreversible inactivation of the enzyme
Mn2+
-
inhibition is completely reversed by EDTA
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-benzyl-N'-[3-(5-methyl-1,3-benzoxazol-2-yl)phenyl]urea
-
N-methyl-3,5-di(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-methyl-5-(1H-pyrrol-3-yl)-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-methyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
p-chloromercuribenzoate
-
-
riboflavin
-
slight inhibition, restoration by FAD
tetracycline
-
inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 0.25 and 0.13 microg/ml
Thiol-blocking reagents
-
tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex
-
binding structure, overview
Zn2+
-
inhibition is completely reversed by EDTA
[2-[(6-chloro-1,2-dihydroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-4,6-dioxo-2,4,6,7-tetrahydro-5H-pyrazolo[3,4-d]pyrimidin-5-yl]acetonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 2 and 1 microg/ml
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.25 mg/l
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
analysis of mouse and human internal clearance
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Enterococcus faecalis
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
-
2-Nitro-5-thiocyanobenzoate
-
-
2-Nitro-5-thiocyanobenzoate
-
complete inactivation at 0.1 mM
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
analysis of mouse and human internal clearance
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
a pyrazolopyrimidinedione analogue identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori, it is time-independent, fully-reversible and insensitive to changes in enzyme or detergent concentration
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 4 microg/ml
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
beta-Chloro-D-alanine
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. BCDA-treated BsMurI has a single cysteine residue, C185, that is the sole site of modification in over 95% of the inactivated protein. BCDA inhibition of MurI is mechanism-based as opposed to arising from nonspecific interaction with suitably configured cysteine thiols
beta-Chloro-D-alanine
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. BCDA modifies MtMurI in vitro and in vivo
dipicolinic acid
-
allosteric inhibitor of both Bacillus anthracis glutamate racemase isozymes which exhibits low micromolar inhibition with clear noncompetitive behavior
FAD
-
and analogs
hydroxylamine
-
-
hydroxylamine
-
different experimentators found inhibition or no inhibition
hydroxylamine
-
no inactivation
Thiol-blocking reagents
-
DL-Glu protects from inactivation
-
Thiol-blocking reagents
-
-
-
additional information
-
the pressure does not affect catalysis after substrate binding
-
additional information
no inhibition by beta-fluoroalanine (BFA, racemic mixture) and O-acetyl-D-serine (OADS)
-
additional information
-
library screening for inhibitory compounds, two Zn (II) and Mn (III) 1,3,5-triazapentadienate complexes are found to efficiently inhibit the glutamate racemase activity. The metal complexes affect the enzyme activity by binding to the enzyme-substrate complex and promoting the formation of an inhibited dimeric form of the enzyme. Evaluation of a series of compounds, including 1H-benzimidazole-2-sulfonic acid, dipicolinic acid, 4-hydroxybenzene-1,3-disulfonate, and (2R)-2-amino-4-benzylpentanedioic acid, which are already known inhibitors of different bacterial glutamate racemases, for inhibitory activity on the enzyme, inhibition mechanism of BcGR by metal complexes, overview
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
-
substrate-product analogue inhibitor synthesis and evaluation, overview
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
although Tris-HCl isthe buffer most commonly employed when assaying glutamate racemases from various microbial sources, FnGR is slightly inhibited in this buffer, kcat values are reduced 14% and 25% in the L-D and D-L reaction directions at pH 8.0, respectively relative to the corresponding values observed using the phosphate assay buffer
-
additional information
-
design of inhibitors of glutamate racemase as selective antibacterial agents, incorporation of imidazoles onto a core pyrazolopyrimidinedione scaffold to improve bioavailabilty, structure-activity relationships, MIC values with wild-type Helicobacter pylori strain 055 and mutant strain hefC-, overview. Substituents on the inhibitor scaffold are varied to optimize target potency, antibacterial activity, and in vivo pharmacokinetic stability
-
additional information
-
insensitive to carbonyl reagents such as hydroxylamine, phenylhydrazine, or NaBH4
-
additional information
no inhibition by beta-fluoroalanine (BFA, racemic mixture) and O-acetyl-D-serine (OADS). MtMurI adopts a unique oligomeric configuration and contains distinct active-site architectural differences from other MurI orthologues and that dimer interface mutations are required to introduce catalytic capability. Conventional MurI inhibitors are inactive against this recombinant form of mycobacterial MurI, the selective inhibitory activity of BCDA against MtMurI may arise from unique protein-ligand interactions unseen in orthologous MurIs. MsMurI results demonstrate these same structural features and yet BCDA does not appear to act via MurI in this bacterium
-
additional information
-
no inhibition by beta-fluoroalanine (BFA, racemic mixture) and O-acetyl-D-serine (OADS). MtMurI adopts a unique oligomeric configuration and contains distinct active-site architectural differences from other MurI orthologues and that dimer interface mutations are required to introduce catalytic capability. Conventional MurI inhibitors are inactive against this recombinant form of mycobacterial MurI, the selective inhibitory activity of BCDA against MtMurI may arise from unique protein-ligand interactions unseen in orthologous MurIs. MsMurI results demonstrate these same structural features and yet BCDA does not appear to act via MurI in this bacterium
-
additional information
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
-
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
development of a class of Mycobacterium tuberculosis (Mtb) inhibitors by exploring the pharmaceutically underexploited enzyme targets which are majorly involved in cell wall biosynthesis of mycobacteria, compoud library screening using a thermal shift assay. Identification of two lead compounds, optimization and expansion result in twenty four compounds. Molecular docking and dynamic studies using the D-glutamate bound glutamate racemase structures of Mycobacterium tuberculosis (PDB ID 5HJ7) and Bacillus subtilis (PDB ID 1ZUW), simulations and modeling, overview. The compounds are also tested on their cytotoxicity and in a Myconacterium tuberculosis biofilm assay, activity profile of compounds in nutrient starved stress model, overview
-
additional information
-
development of a class of Mycobacterium tuberculosis (Mtb) inhibitors by exploring the pharmaceutically underexploited enzyme targets which are majorly involved in cell wall biosynthesis of mycobacteria, compoud library screening using a thermal shift assay. Identification of two lead compounds, optimization and expansion result in twenty four compounds. Molecular docking and dynamic studies using the D-glutamate bound glutamate racemase structures of Mycobacterium tuberculosis (PDB ID 5HJ7) and Bacillus subtilis (PDB ID 1ZUW), simulations and modeling, overview. The compounds are also tested on their cytotoxicity and in a Myconacterium tuberculosis biofilm assay, activity profile of compounds in nutrient starved stress model, overview
-
additional information
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
-
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
-
no inactivation by carbonyl reagents such as hydroxylamine and NaBH4
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
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24.1
(R,S)-1-hydroxy-1-oxo-4-amino-4-carboxyphosphorinane
Enterococcus faecalis
-
pH and temperature not specified in the publication
215
(R,S)-4-amino-4-carboxy-1,1-dioxotetrahydro-thiopyran
Enterococcus faecalis
-
pH and temperature not specified in the publication
21.2
1,1-dioxo-tetrahydrothiopyran-4-one
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.0068
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.0088
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylurea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)thiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.0115
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)urea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.0011
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)thiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.00182
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)urea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-methoxyphenyl)urea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.0044
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)urea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.00835
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)urea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.0013
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylthiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylurea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.00712
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-isopropylurea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylurea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.0228
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.0085
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-methoxyphenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-benzyl-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
47.7
1-hydroxyphosphinan-4-one 1-oxide
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.0009 - 0.0038
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
0.0014 - 0.0025
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
0.0022 - 0.0026
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
0.007 - 0.4
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
105
2-amino-4-phosphonobutanoic acid
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.000026 - 0.0027
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
0.000033
2-[(5-chloro-1-methyl-1H-indol-3-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
0.000069
2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000079
2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00017
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-7-(2-methylpropyl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00026
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-3-(1-methyl-1H-pyrrol-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00046
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(pent-4-yn-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000056
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-en-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000024
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-yn-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00022
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(propan-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00017
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000054
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(3-hydroxyprop-2-yn-1-yl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000072
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00081
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-1,2,4-triazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000041
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0009
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00022
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-pyrazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00023
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-4H-1,2,4-triazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
0.00015
2-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00025
2-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00025
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000089
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00018
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000087
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00074
3-(2-amino-4-methyl-1,3-thiazol-5-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00028
3-(2-amino-5-methyl-1,3-thiazol-4-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0028
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.000039
3-(4-acetyl-1-methyl-1H-pyrrol-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.007
3-(5-methylbenzo[d]oxazol-2-yl)aniline
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
-
0.025
3-(benzo[d]oxazol-2-yl)aniline
Mycobacterium tuberculosis
above, pH 8.0, 37°C, recombinant enzyme
-
2.9
3-sulfobenzoic acid
Bacillus subtilis
structural analogue of dipicolinate dianion
0.0015 - 0.0031
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
0.00065 - 0.0015
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
0.0011 - 0.0035
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
0.0076 - 0.021
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
0.0024 - 0.0064
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
0.0019 - 0.052
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
0.00022
4-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-5-methylfuran-2-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000063
5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.002
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.0014
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-(pyridin-4-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000062
5-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000055
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-(cyanomethyl)-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00008
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000086
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00007
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000028
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00024
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(propan-2-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00067
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-1,2,3-triazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00047
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-pyrazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000013
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-1,2,4-triazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00012
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-pyrazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000088
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(2-hydroxyethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000057
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(4-hydroxybut-2-yn-1-yl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00007
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000026
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00006
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-4-methylfuran-2-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00026
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(1H-imidazol-1-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000051
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000016
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-[5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl]-1H-pyrrole-3-sulfonamide
Helicobacter pylori
-
0.000074
5-[5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00016
5-[5-(but-3-yn-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0043 - 0.0044
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
0.0353
bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex
Burkholderia cenocepacia
-
recombinant enzyme, pH 8.0, 37°C
-
60.4
bis(2-carboxyethyl)-phosphinic acid
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.15
dipicolinic acid
Burkholderia cenocepacia
-
recombinant enzyme, pH 8.0, 37°C
0.0044 - 0.361
exiguaquinol
0.0017
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.00625
N-benzyl-N'-[3-(5-methyl-1,3-benzoxazol-2-yl)phenyl]urea
Mycobacterium tuberculosis
pH 8.0, 37°C, recombinant enzyme
0.0007
N-methyl-3,5-di(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.0006
N-methyl-5-(1H-pyrrol-3-yl)-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.0022
N-methyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
0.0014 - 0.4
pyrazolopyrimidinedione analogue
-
0.01
tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex
Burkholderia cenocepacia
-
recombinant enzyme, pH 8.0, 37°C
0.0009
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0038
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0014
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Enterococcus faecalis
-
0.0025
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Enterococcus faecium
-
0.0022
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Enterococcus faecalis
-
0.0026
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Enterococcus faecium
-
0.007
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
Enterococcus faecalis
-
-
0.018
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
Enterococcus faecium
-
-
0.4
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
Staphylococcus aureus
-
-
0.000026
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Helicobacter pylori
-
0.002
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Enterococcus faecalis
-
0.0027
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Enterococcus faecium
-
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0015
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0031
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.00065
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0015
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0011
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0035
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0076
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.021
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0024
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0064
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0019
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.052
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0043
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Enterococcus faecalis
-
0.0044
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Enterococcus faecium
-
0.0044
exiguaquinol
Helicobacter pylori
-
substrate D-serine-O-sulfate
0.361
exiguaquinol
Helicobacter pylori
-
substrate D-glutamate
0.0014
pyrazolopyrimidinedione analogue
Helicobacter pylori
-
a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori, it is time-independent, fully-reversible and insensitive to changes in enzyme or detergent concentration
-
0.4
pyrazolopyrimidinedione analogue
Escherichia coli
-
value above 0.4, a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori but not for MurI of Escherichia coli
-
0.4
pyrazolopyrimidinedione analogue
Staphylococcus aureus
-
value above 0.4, a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori but not for MurI of Staphylococcus aureus
-
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evolution
-
a large number of Chlamydia species (as well as members of the Planctomycetes-Verrucomicrobiae-Chlamydiae superphylum) possess DapF but lack homologues of MurI. It is likely that DapF is a primordial isomerase that functions as both racemase and epimerase in these organisms, suggesting that specialized D-glutamate racemase enzymes never evolved in these microbes. DapFCT possesses an additional cysteine (C86) that is not highly conserved in other bacterial species
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
evolution
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria. Primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining
-
malfunction
inactivation of glutamate racemase eliminates the virulence in Streptococcus mutans, a stable mutant of Streptococcus mutans deficient in glutamate racemase, strain FW1718, is constructed to investigate the impact of murI inactivation on cariogenic virulence in wild-type strain UA159. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance related gene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
malfunction
Q81LA8, Q81UL8
the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable
malfunction
-
inactivation of glutamate racemase eliminates the virulence in Streptococcus mutans, a stable mutant of Streptococcus mutans deficient in glutamate racemase, strain FW1718, is constructed to investigate the impact of murI inactivation on cariogenic virulence in wild-type strain UA159. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance related gene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
-
malfunction
-
the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable
-
metabolism
-
D-glutamate is generated via the racemization of L-glutamate by glutamate racemase (MurI). Chlamydia lacks homologues of MurI. The bifunctional diaminopimelate epimerase (DapF) also synthesizes D-glutamate, EC 5.1.1.3, and catalyzes the final step in the synthesis of meso-diaminopimelate, an amino acid unique to peptidoglycan, EC 5.1.1.7
metabolism
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
metabolism
-
several bacteria with reduced genomes lack alr, encoding alanine racemase, but contain metC encoding cystathionine beta-lyase (CBL, EC 4.4.1.13), which, in these organisms, is a multifunctional CBL/ALR. CBL activity is no longer required in these bacteria
-
physiological function
-
essential enzyme in peptidoglycan biosynthesis
physiological function
peptidoglycan biosynthesis
physiological function
-
peptidoglycan synthesis
physiological function
-
peptidoglycan synthesis
physiological function
peptidoglycan synthesis
physiological function
peptidoglycan synthesis
physiological function
-
glutamate racemase catalyzes stereoinversion at the Calpha of glutamate and is a source of D-glutamate in bacteria, an essential component of the peptidoglycan layer of the bacterial cell walls
physiological function
-
overexpression of the glutamate racemase gene not only increases the production of poly-gamma-glutamic acid by 22.5% but also increases the proportion of D-glutamate in poly-gamma-glutamic acid from 77 to 85%
physiological function
-
D-glutamate is an essential biosynthetic building block of the peptidoglycans that encapsulate the bacterial cell wall
physiological function
-
glutamate racemase provides D-glutamate for the construction of N-acetylglucosamine-N-acetylmuramic acid peptidoglycan subunits assimilated into the bacterial cell wall
physiological function
-
DapF is a primordial isomerase that functions as both racemase and epimerase in the organism. genetic complementation of an Escherichia coli murI mutant demonstrating that Chlamydia DapF can generate D-glutamate. D-Glu racemase activity is required for synthesizing D-Glu-containing peptidoglycan, DapFCT is also capable of racemizing D-Glu to L-Glu
physiological function
enzyme MurI function is essential for the growth of Mycobacterium tuberculosis cells
physiological function
Q81LA8, Q81UL8
genes racE1 and racE2, encoding two glutamate racemases, are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
physiological function
Q81LA8, Q81UL8
genes racE1 and racE2, encoding two glutamate racemases,are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
physiological function
glutamate racemase (GR) catalyzes the cofactor independent stereoinversion of L- to D-glutamate for biosynthesis of bacterial cell walls. Glutamate racemase is a flexible enzyme capable of binding a variety of small molecules both in the active site and at allosteric binding pockets
physiological function
glutamate racemase (MurI) is an essential enzyme in peptidoglycan biosynthesis
physiological function
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
physiological function
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
physiological function
-
glutamate racemase is an essential enzyme for the biosynthesis of the bacterial cell wall
physiological function
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
physiological function
MurI is essential for growth, and glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in Mycobacterium smegmatis
physiological function
-
glutamate racemase (GR) catalyzes the cofactor independent stereoinversion of L- to D-glutamate for biosynthesis of bacterial cell walls. Glutamate racemase is a flexible enzyme capable of binding a variety of small molecules both in the active site and at allosteric binding pockets
-
physiological function
-
glutamate racemase (MurI) is an essential enzyme in peptidoglycan biosynthesis
-
physiological function
-
overexpression of the glutamate racemase gene not only increases the production of poly-gamma-glutamic acid by 22.5% but also increases the proportion of D-glutamate in poly-gamma-glutamic acid from 77 to 85%
-
physiological function
-
glutamate racemase provides D-glutamate for the construction of N-acetylglucosamine-N-acetylmuramic acid peptidoglycan subunits assimilated into the bacterial cell wall
-
physiological function
-
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
-
physiological function
-
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
-
physiological function
-
enzyme MurI function is essential for the growth of Mycobacterium tuberculosis cells
-
physiological function
-
genes racE1 and racE2, encoding two glutamate racemases, are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
-
physiological function
-
genes racE1 and racE2, encoding two glutamate racemases,are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
-
physiological function
-
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
-
physiological function
-
MurI is essential for growth, and glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in Mycobacterium smegmatis
-
additional information
-
mechanism of Helicobacter pylori glutamate racemase to generate the thermodynamically unfavorable reverse protonation state of the catalytic residue cysteine required for the proton abstraction from the alpha-carbon of glutamate, molecular dynamics simulations with a molecular mechanics force field along with QM/MM calculations starting from the crystal structure and from different MD snapshot, structural fluctuations of the enzyme-substrate complex, structural analysis of the four transition state structures,overview
additional information
MurI from Lactobacillus plantarum NC8 seems to exhibit pseudosymmetry for the racemisation of Glu in both directions
additional information
molecular dynamics simulations on the enzyme have suggested particular regions that undergo relatively large changes, both in terms of substrate unbinding, as well as equilibrated enzyme-ligand complexes that show movement relative to one another (i.e., enzyme complexes with different types of active site small molecules equilibrated to distinct conformers)
additional information
-
structure homology modeling, in BcGR, all critical residues for enzymatic activity and substrate recognition are fully conserved within the 2-domain glutamate racemase fold
additional information
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
-
the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview. DapFCT requires the epimerase active-site cysteines for glutamate racemase activity
additional information
-
molecular dynamics simulations on the enzyme have suggested particular regions that undergo relatively large changes, both in terms of substrate unbinding, as well as equilibrated enzyme-ligand complexes that show movement relative to one another (i.e., enzyme complexes with different types of active site small molecules equilibrated to distinct conformers)
-
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
-
additional information
-
MurI from Lactobacillus plantarum NC8 seems to exhibit pseudosymmetry for the racemisation of Glu in both directions
-
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
-
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D7S
turnover number is decreased by 170fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 6fold compared to wild-type enzyme in the L to D reaction
E147N
turnover number is decreased by 100fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 7fold compared to wild-type enzyme in the L to D reaction
C185A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C188A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C74A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C77A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
K29A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
P99A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
Q86A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R214A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R214A/K106A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R25A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
S207A
-
the isozyme RacE2 mutant is insensitive to dipicolinic acid
V149A
-
mutant V149A has about a 2fold higher kcat than wild-type RacE2 (67/sec versus 38/sec), and has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM), in the reverse reaction, V149A has a higher kcat than RacE2 (4.9/sec versus 1.6/sec, respectively), and its Km value for D-glutamate is the same as that of RacE2 (0.2 mM)
Y221A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
T76A
production by site-directed mutagenesis, strong RacE-glutamate carbanion interaction energy is notably dissipated with the mutant
V149A
while V149A BsGR exhibits a 3- and 6fold increase in the value of Km for L- and D-glutamate relative to wild-type BsGR, respectively, the values of kcat are slightly increased relative to the wild-type enzyme
A151V
production by site-directed mutagenesis, alanine ist essential for activity, mutation of residue 151 located at the entryway to the active site reveals that FnGR is very sensitive to increased steric bulk at this position
A75T
-
Ki: 0.661 mM (inhibitor: D-glutamate). Turnover number: 1.78/sec (substrate: L-glutamate), 0.065/sec (substrate: D-glutamate). Km: 7.4 mM (substrate: L-glutamate), Km: 0.275 mM (substrate: D-glutamate)
E151T
-
Ki: 100 mM (value above 100 for inhibitor: D-glutamate). Turnover number: 0.08/sec (substrate: D-glutamate), 2.26/sec (substrate: L-glutamate). Km: 7.36 mM (substrate: L-glutamate), Km: 0.282 mM (substrate: D-glutamate)
C184A
-
mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme
C73A
-
mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme
D10N
-
1015fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.9fold increase in Km-value for L-glutamate compared to wild-type enzyme. 1079fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 4.6fold increase in Km-value for D-glutamate compared to wild-type enzyme
D36N
-
3.4fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 106fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 158fold increase in Km-value for D-glutamate compared to wild-type enzyme
E152Q
-
1.8fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.1fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 13.5fold increase in Km-value for D-glutamate compared to wild-type enzyme
H186N
-
1533fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.4fold increase in Km-value for L-glutamate compared to wild-type enzyme. 731fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 17.3fold increase in Km-value for D-glutamate compared to wild-type enzyme
C185S
-
decrease in racemization activity, mutant retains its gyrase inhibition ability
C75S
-
decrease in racemization activity, mutant retains its gyrase inhibition ability
C75SC185S
-
less than 10% of wild-type activity, mutant retains its gyrase inhibition ability
D26R/R105A/G194E
site-directed mutagenesis, mutation of the interface affording a soluble and active enzyme
D26R/R105A/G194R
site-directed mutagenesis, mutation of the interface affording a soluble and active enzyme
D26R/R105A/G194E
-
site-directed mutagenesis, mutation of the interface affording a soluble and active enzyme
-
D26R/R105A/G194R
-
site-directed mutagenesis, mutation of the interface affording a soluble and active enzyme
-
K106A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
K106A
-
the isozyme RacE2 mutant is insensitive to dipicolinic acid
additional information
Q81LA8
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
additional information
Q81UL8
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
additional information
-
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
additional information
Q81LA8
using allelic replacement, chromosomal racE2 is replaced with the spectinomycin resistance gene (aad9) and transduced via bacteriophage CP-51 into Bacillus anthracis strain Sterne, generating strain SYO2 (DELTAracE2::aad9)
additional information
Q81UL8
using allelic replacement, chromosomal racE2 is replaced with the spectinomycin resistance gene (aad9) and transduced via bacteriophage CP-51 into Bacillus anthracis strain Sterne, generating strain SYO2 (DELTAracE2::aad9)
additional information
-
using allelic replacement, chromosomal racE2 is replaced with the spectinomycin resistance gene (aad9) and transduced via bacteriophage CP-51 into Bacillus anthracis strain Sterne, generating strain SYO2 (DELTAracE2::aad9)
additional information
-
using allelic replacement, chromosomal racE2 is replaced with the spectinomycin resistance gene (aad9) and transduced via bacteriophage CP-51 into Bacillus anthracis strain Sterne, generating strain SYO2 (DELTAracE2::aad9)
-
additional information
-
disruption of enzyme gene yrpC, no effect on growth or production of poly-gamma-glutamte. Disruption of enzyme gene glr, cells are only viable when an exogenous gene copy is present on a plasmid. Glr gene product is responsible for supply of D-glutamate both to the synthesis of peptidoglycan and poly-gamma-glutamate
additional information
-
enzyme knockout mutants, gene racE is essential for growth in rich medium but dispensable for growth in minimal medium. YrpC gene is expressed only in minimal medium. Neither gene is required for synthesis of poly-gamma-DL-glutamate. RacE or yrpC mutant cells accumulate signifcant amounts of D- but not L-glutamate. RacE/yrpC double mutant shows severely impaired D-amino acid utilization
additional information
Tyr53 mutated to the L-(7-hydroxycoumarin-4-yl) ethylglycine (7HC) functional group by site-directed mutagenesis provides ligand-associated fluorescent sensitivity to changes in the local environment (and thus serve as an allosteric reporter), without sacrificing particular contacts with ligands. The placement of the 7HC moiety at the surface of the enzyme, mutant GRY53/7HC mutant, remote from any ligand pockets, places it in a microenvironment where dielectric values are significantly larger, which restricts fluorescence changes to largely water polarization effects. The extraordinary sensitivity of the 7HC moiety within GRY53/7HC, and its incorporation into the dynamic region, provides a valuable experimental probe, quickly identifying a more open and solvated form, which is umwanted for high quality complexation. The GRY53/7HC mutant maintains the same KM value as the wild-type enzyme, but exhibits a 40fold decreased kcat
additional information
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Tyr53 mutated to the L-(7-hydroxycoumarin-4-yl) ethylglycine (7HC) functional group by site-directed mutagenesis provides ligand-associated fluorescent sensitivity to changes in the local environment (and thus serve as an allosteric reporter), without sacrificing particular contacts with ligands. The placement of the 7HC moiety at the surface of the enzyme, mutant GRY53/7HC mutant, remote from any ligand pockets, places it in a microenvironment where dielectric values are significantly larger, which restricts fluorescence changes to largely water polarization effects. The extraordinary sensitivity of the 7HC moiety within GRY53/7HC, and its incorporation into the dynamic region, provides a valuable experimental probe, quickly identifying a more open and solvated form, which is umwanted for high quality complexation. The GRY53/7HC mutant maintains the same KM value as the wild-type enzyme, but exhibits a 40fold decreased kcat
-
additional information
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site-directed mutagenesis experiments are described demonstrating the participation of Cys96 and Cys208 in the two-base reaction mechanism of the enzyme. The construction of N-terminal-truncated or C-terminal-truncated enzymes shows that the characteristic N-terminal amino acid extension of 20 residues is not involved in its activation by the nucleotide precursor
additional information
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with 0.0065 mM UDP-N-acetylmuramoyl-L-Ala added, the N-terminal truncated enzyme displays a loss of more than 80% of the activity compared to the full-length enzyme
additional information
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overexpression in vivo provides resistance to the action of ciprofloxacin
additional information
gene murI deletion in the chromosome, phenotype. In the absence of MurI, no other proteins are able to complement its function in the cell, method, overview
additional information
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gene murI deletion in the chromosome, phenotype. In the absence of MurI, no other proteins are able to complement its function in the cell, method, overview
additional information
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gene murI deletion in the chromosome, phenotype. In the absence of MurI, no other proteins are able to complement its function in the cell, method, overview
-
additional information
generation of a DELTAmurI strain of Mycobacterium smegmatis, the deletion of the murI gene can be achieved only in minimal medium supplemented with D-glutamate. Gene murI deletion via the gene replacement vector, pKKYL02, temperature-sensitive vector propagation and allelic exchange mutagenesis. Phenotype of DELTAmurI mutant strains on solid minimal medium, DELTAmurI mutant cells display a morphology different from the wild-type cells with pear-shaped swellings at their polar ends, overview
additional information
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generation of a DELTAmurI strain of Mycobacterium smegmatis, the deletion of the murI gene can be achieved only in minimal medium supplemented with D-glutamate. Gene murI deletion via the gene replacement vector, pKKYL02, temperature-sensitive vector propagation and allelic exchange mutagenesis. Phenotype of DELTAmurI mutant strains on solid minimal medium, DELTAmurI mutant cells display a morphology different from the wild-type cells with pear-shaped swellings at their polar ends, overview
additional information
site-directed mutagenesis of the enzyme's interface affording a soluble and active enzyme
additional information
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site-directed mutagenesis of the enzyme's interface affording a soluble and active enzyme
additional information
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site-directed mutagenesis of the enzyme's interface affording a soluble and active enzyme
-
additional information
-
generation of a DELTAmurI strain of Mycobacterium smegmatis, the deletion of the murI gene can be achieved only in minimal medium supplemented with D-glutamate. Gene murI deletion via the gene replacement vector, pKKYL02, temperature-sensitive vector propagation and allelic exchange mutagenesis. Phenotype of DELTAmurI mutant strains on solid minimal medium, DELTAmurI mutant cells display a morphology different from the wild-type cells with pear-shaped swellings at their polar ends, overview
-
additional information
inactivation of MurI eliminating the virulence in Streptococcus mutans. The length, width and height of strain FW1718 cells are increased by 1.7, 2.6, and 1.7fold, respectively. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance relatedgene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
additional information
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inactivation of MurI eliminating the virulence in Streptococcus mutans. The length, width and height of strain FW1718 cells are increased by 1.7, 2.6, and 1.7fold, respectively. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance relatedgene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
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364-373
2015
Bacillus subtilis (P94556), Bacillus subtilis 168 (P94556)
brenda
Prosser, G.A.; Rodenburg, A.; Khoury, H.; de Chiara, C.; Howell, S.; Snijders, A.P.; de Carvalho, L.P.
Glutamate racemase is the primary target of beta-chloro-D-alanine in Mycobacterium tuberculosis
Antimicrob. Agents Chemother.
60
6091-6099
2016
Bacillus subtilis (P94556), Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis, Bacillus subtilis 168 (P94556), Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9)
brenda
Poen, S.; Nakatani, Y.; Opel-Reading, H.K.; Lasse, M.; Dobson, R.C.; Krause, K.L.
Exploring the structure of glutamate racemase from Mycobacterium tuberculosis as a template for anti-mycobacterial drug discovery
Biochem. J.
473
1267-1280
2016
Mycolicibacterium smegmatis (A0R1X0), Mycolicibacterium smegmatis, Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9), Mycolicibacterium smegmatis ATCC 700084 / mc(2)155 (A0R1X0)
brenda
Malapati, P.; Krishna, V.S.; Nallangi, R.; Srilakshmi, R.R.; Sriram, D.
Identification and development of benzoxazole derivatives as novel bacterial glutamate racemase inhibitors
Eur. J. Med. Chem.
145
23-34
2018
Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9)
brenda
Morayya, S.; Awasthy, D.; Yadav, R.; Ambady, A.; Sharma, U.
Revisiting the essentiality of glutamate racemase in Mycobacterium tuberculosis
Gene
555
269-276
2015
Mycobacterium tuberculosis (P9WPW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WPW9)
brenda
Li, Y.; Mortuza, R.; Milligan, D.L.; Tran, S.L.; Strych, U.; Cook, G.M.; Krause, K.L.
Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis
J. Bacteriol.
196
4239-4244
2014
Mycolicibacterium smegmatis (A0R1X0), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 700084 / mc(2)155 (A0R1X0)
brenda
Oh, S.Y.; Richter, S.G.; Missiakas, D.M.; Schneewind, O.
Glutamate racemase mutants of Bacillus anthracis
J. Bacteriol.
197
1854-1861
2015
Bacillus anthracis (Q81LA8), Bacillus anthracis (Q81UL8), Bacillus anthracis, Bacillus anthracis Sterne 34F2 (Q81LA8), Bacillus anthracis Sterne 34F2 (Q81UL8)
brenda
Liechti, G.; Singh, R.; Rossi, P.; Gray, M.; Adams, N.; Maurelli, A.
Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase activities
mBio
9
pii: e00204-18
2018
Chlamydia trachomatis
brenda
Zhang, J.; Liu, J.; Ling, J.; Tong, Z.; Fu, Y.; Liang, M.
Inactivation of glutamate racemase (MurI) eliminates virulence in Streptococcus mutans
Microbiol. Res.
186-187
1-8
2016
Streptococcus mutans serotype c (Q8DSQ5), Streptococcus mutans serotype c ATCC 700610 / UA159 (Q8DSQ5)
brenda
Israyilova, A.; Buroni, S.; Forneris, F.; Scoffone, V.C.; Shixaliyev, N.Q.; Riccardi, G.; Chiarelli, L.R.
Biochemical characterization of glutamate racemase - a new candidate drug target against Burkholderia cenocepacia infections
PLoS ONE
11
e0167350
2016
no activity in Homo sapiens, Burkholderia cenocepacia
brenda
Ferla, M.P.; Brewster, J.L.; Hall, K.R.; Evans, G.B.; Patrick, W.M.
Primordial-like enzymes from bacteria with reduced genomes
Mol. Microbiol.
105
508-524
2017
Wolbachia pipientis (Q73GL9), Thermotoga maritima (Q9X0Z7), Wolbachia pipientis wMel (Q73GL9), Thermotoga maritima DSM 3109 (Q9X0Z7), Thermotoga maritima ATCC 43589 (Q9X0Z7), Thermotoga maritima JCM 10099 (Q9X0Z7)
brenda