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adipyl-L-cysteinyl-D-valine + ?
N-(4-carboxybutyl)penicillin + 2 H2O
-
-
-
-
?
delta-(L-alpha-aminoadipoyl)-(3R)-methyl-L-cysteine D-alpha hydroxyvaleryl ester + O2
? + H2O
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
(2S)-2-amino-6-([(2R)-1-[(1S)-1-carboxy-2-methylpropoxy]-1,3-dioxo-3-sulfanylpropan-2-yl]amino)-6-oxohexanoic acid + H2O
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-beta-methyl-D-cyclopropylglycine + O2
(2R,8R)-8-([(5S)-5-amino-5-carboxypentanoyl]amino)-3-methylene-9-oxo-6-thia-1-azabicyclo[5.2.0]nonane-2-carboxylic acid + H2O
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-hydroxyisovaleryl ester + O2
?
-
for this substrate analogue (ACOV) lacking an amide nitrogen IPNS exhibits oxygenase activity
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2
(2S,3S,5R,6R)-6-[[(5S)-5-amino-5-carboxypentanoyl]amino]-3-methoxy-3-methyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2 H2O
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-cysteine + O2
(4S,7S)-7-[[(5S)-5-amino-5-carboxypentanoyl]amino]-6-oxohexahydropyrrolo[2,1-c][1,2,4]dithiazine-4-carboxylic acid + 2 H2O
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine + O2
(2S)-2-amino-6-([(3S)-1-[(1R)-1-carboxy-2-methylpropyl]-5-hydroxy-2-oxopyrrolidin-3-yl]mino)-6-oxohexanoic acid + ?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine + O2
?
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-alpha-aminobutyrate + O2
?
-
wild-type and mutants, reaction mechanism
-
-
ir
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
delta-L-alpha-aminoadipoyl-L-cysteine (1-(S)-carboxy-2-thiomethyl)ethyl ester + O2
? + H2O
-
substrate analogue
-
-
?
delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
?
-
-
-
?
delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
? + H2O
-
-
-
-
?
L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
(2S)-2-amino-6-([(2S)-1-[(carboxymethyl)amino]-3,3-dihydroxy-1-oxopropan-2-yl]amino)-6-oxohexanoic acid + H2O
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin + H2O
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
N6-[(1R,2S)-1-([[(1R)-1-carboxy-2-methylpropyl]oxy]carbonyl)-2-sulfanylpropyl]-6-oxo-L-lysine + O2
? + H2O
substrate analogue
-
-
?
phenylacetyl-L-cysteinyl-D-valine + O2
penicillin G + 2 H2O
-
-
-
-
?
additional information
?
-
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
(2S)-2-amino-6-([(2R)-1-[(1S)-1-carboxy-2-methylpropoxy]-1,3-dioxo-3-sulfanylpropan-2-yl]amino)-6-oxohexanoic acid + H2O
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
(2S)-2-amino-6-([(2R)-1-[(1S)-1-carboxy-2-methylpropoxy]-1,3-dioxo-3-sulfanylpropan-2-yl]amino)-6-oxohexanoic acid + H2O
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
?
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteine D-alpha-hydroxyisovaleryl ester + O2
?
-
-
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2
(2S,3S,5R,6R)-6-[[(5S)-5-amino-5-carboxypentanoyl]amino]-3-methoxy-3-methyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2 H2O
-
product is a bioactive penam. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine is not turned over by the enzyme
-
?
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-allo-threonine + O2
(2S,3S,5R,6R)-6-[[(5S)-5-amino-5-carboxypentanoyl]amino]-3-methoxy-3-methyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid + 2 H2O
-
product is a bioactive penam. Epimeric delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine is not turned over by the enzyme
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-cysteine + O2
(4S,7S)-7-[[(5S)-5-amino-5-carboxypentanoyl]amino]-6-oxohexahydropyrrolo[2,1-c][1,2,4]dithiazine-4-carboxylic acid + 2 H2O
-
product is a bicyclic gamma-lactam disulfide
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-cysteine + O2
(4S,7S)-7-[[(5S)-5-amino-5-carboxypentanoyl]amino]-6-oxohexahydropyrrolo[2,1-c][1,2,4]dithiazine-4-carboxylic acid + 2 H2O
-
product is a bicyclic gamma-lactam disulfide
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine + O2
(2S)-2-amino-6-([(3S)-1-[(1R)-1-carboxy-2-methylpropyl]-5-hydroxy-2-oxopyrrolidin-3-yl]mino)-6-oxohexanoic acid + ?
-
enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine + O2
(2S)-2-amino-6-([(3S)-1-[(1R)-1-carboxy-2-methylpropyl]-5-hydroxy-2-oxopyrrolidin-3-yl]mino)-6-oxohexanoic acid + ?
-
enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine + O2
?
-
enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation
-
?
delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-delta-S-methylcysteine + O2
?
-
enzyme converts the homologated tripeptides delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-valine and delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-allylglycine into monocyclic hydroxy-lactam products, suggesting that the additional methylene unit in these substrates induces conformational changes that preclude second ring closure after initial lactam formation
-
?
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
r
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
r
delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
r
delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
for the native substrate IPNS shows oxidase activity
-
-
?
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
(2S)-2-amino-6-([(2S)-1-[(carboxymethyl)amino]-3,3-dihydroxy-1-oxopropan-2-yl]amino)-6-oxohexanoic acid + H2O
-
-
-
?
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
(2S)-2-amino-6-([(2S)-1-[(carboxymethyl)amino]-3,3-dihydroxy-1-oxopropan-2-yl]amino)-6-oxohexanoic acid + H2O
-
-
-
?
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
?
-
-
-
?
L-delta-(alpha-aminoadipoyl)-L-cysteinyl-glycine + O2
?
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin + H2O
-
the enzyme catalyzes the four electron oxidative double ring closure of its substrate
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
involved in biosynthesis of cephalosporin C
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
involved in biosynthesis of cephalosporin C
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
IPNSs are nonheme iron-dependent oxygenases that catalyze cyclization
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
catalytic reaction is under steric regulation
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
evaluation of culture conditions for penicillin and cephalosporin C production
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
additional information
?
-
-
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate is converted to 3 different products: an alpha- and a beta-methyl-penam, and a cepham
-
-
?
additional information
?
-
-
iron-mediated conversion of metal-bound thiolate to sulfenate in crystallographic studies
-
-
?
additional information
?
-
-
in Penicillium chrysogenum, the enzymes involved in penicillin production are compartmentalized in the cytosol and in microbodies
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
adipyl-L-cysteinyl-D-valine + ?
N-(4-carboxybutyl)penicillin + 2 H2O
-
-
-
-
?
delta-L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
?
L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
? + H2O
-
-
-
-
?
L-alpha-aminoadipoyl-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
phenylacetyl-L-cysteinyl-D-valine + O2
penicillin G + 2 H2O
-
-
-
-
?
additional information
?
-
-
in Penicillium chrysogenum, the enzymes involved in penicillin production are compartmentalized in the cytosol and in microbodies
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
involved in biosynthesis of cephalosporin C
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
involved in biosynthesis of cephalosporin C
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
IPNSs are nonheme iron-dependent oxygenases that catalyze cyclization
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
catalytic reaction is under steric regulation
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
modifications of the L-cysteine residue in the second position of the enzyme result in tripeptides that are unable to serve as substrates
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
evaluation of culture conditions for penicillin and cephalosporin C production
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
key enzyme of the biosynthetic pathway
product has antibiotic activity
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
-
common step in the biosynthesis of penicillins, cephalosporins and cephamycins
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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C106S
-
site-directed mutagenesis, 63% reduced activity, 14fold increased Km for N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
C106S/C255S
-
site-directed mutagenesis, 63% reduced activity, 14fold increased Km for N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
C255S
-
site-directed mutagenesis, 33% reduced activity, 1.4fold increased Km for N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
H116L
-
site-directed mutagenesis, reduced activity
H126L
-
site-directed mutagenesis, reduced activity
H137L
-
site-directed mutagenesis, reduced activity
H262L
-
site-directed mutagenesis, complete loss of activity
H272L
-
site-directed mutagenesis, complete loss of activity
H49L
-
site-directed mutagenesis, complete loss of activity
H64L
-
site-directed mutagenesis, reduced activity
P285L
-
site-directed mutagenesis, complete loss of activity, increased soluble expression in Escherichia coli host
Q227L
-
site-directed mutagenesis, 55.10% remaining activity compared to wild-type
Q337L
-
site-directed mutagenesis, slightly reduced activity compared to wild-type
Q230L
-
mutant of IPNS shows diminished enzyme activity, residue is highly conserved among dioxygenases and proximal to the active site, is the fourth ligand for the Fe2+ atom
D216E
-
mutant, retains 1% activity
K98E
the mutant shows about 8% of wild type activity
L223A
-
reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate is a poor substrate
L231I
the mutant shows about 35% of wild type activity
L231V
the mutant shows about 25% of wild type activity
P283A
the mutant shows about 12% of wild type activity
P283I
the mutant shows about 10% of wild type activity
P283V
the mutant shows about 9% of wild type activity
V272T
the mutant shows about 27% of wild type activity
L223I
-
the mutant shows about 33% of wild type activity
-
L223V
-
the mutant shows about 33% of wild type activity
-
L231I
-
the mutant shows about 35% of wild type activity
-
L231V
-
the mutant shows about 25% of wild type activity
-
C104S
-
single-strand-site-directed mutagenesis, loss of more than 96% activity
C142S
-
single-strand-site-directed mutagenesis, loss of 24% activity
C251S
-
single-strand-site-directed mutagenesis, loss of 47.7% activity
C37S
-
single-strand-site-directed mutagenesis, loss of 18.3% activity
C37S/C142S/C251S
-
triple mutant, conformationally different from wild-type, prepared by recombining fragments of IPNS-encoding gene pcbC from each of the single mutants, loss of more than 90% activity
D214C
-
site-directed mutagenesis, active site mutant, complete loss of activity
D214E
-
site-directed mutagenesis, active site mutant, retains 1% of activity compared to wild-type
H212D
-
site-directed mutagenesis, active site mutant, complete loss of activity
H212N
-
site-directed mutagenesis, active site mutant, complete loss of activity
H212Q
-
site-directed mutagenesis, active site mutant, complete loss of activity
H268D
-
site-directed mutagenesis, active site mutant, complete loss of activity
H268N
-
site-directed mutagenesis, active site mutant, complete loss of activity
H268Q
-
site-directed mutagenesis, active site mutant, complete loss of activity
L223I
-
reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, product spectrum differs from that of the wild-type with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate
L223I
the mutant shows about 33% of wild type activity
L223V
-
reduced activity with N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine, product spectrum differs from that of the wild-type with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate as substrate
L223V
the mutant shows about 33% of wild type activity
D214H
-
site-directed mutagenesis, complete inactive enzyme
D214H
-
site-directed mutagenesis, active site mutant, complete loss of activity
additional information
-
exchange of Asp214 and His268, and exchange of Asp214 and His 212 by site-directed mutagenesis leads to completely inactive enzymes
additional information
-
exchange of Asp214 and His268, and exchange of Asp214 and His 212 by site-directed mutagenesis leads to completely inactive enzymes
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Castro, J.M.; Liras, P.; Laiz, L.; Cortes, J.; Martin, J.F.
Purification and characterization of the isopenicillin N synthase of Streptomyces lactamdurans
J. Gen. Microbiol.
134
133-141
1988
Acremonium chrysogenum, Amycolatopsis lactamdurans, Penicillium chrysogenum
brenda
Rollins, M.J.; Jensen, S.E.; Westlake, D.W.S.
Isopenicillin N synthase and desacetoxycephalosporin C synthase activities during defined medium fermentations of Streptomyces clavuligerus: effect of oxygen and iron supplements
Can. J. Microbiol.
35
1111-1117
1989
Streptomyces clavuligerus
brenda
Palissa, H.; Von Doehren, H.; Kleinkauf, H.; Ting, H.H.; Baldwin, J.E.
beta-Lactam biosynthesis in a Gram-negative eubacterium: purification and characterization of isopenicillin N synthase from Flavobacterium sp. strain SC 12.154
J. Bacteriol.
171
5720-5728
1989
Flavobacterium sp., Flavobacterium sp. SC 12.154
brenda
Kriauciunas, A.; Frolik, C.A.; Hassell, T.C.; Skatrud, P.L.; Johnson, M.G.; Holbrook, N.L.; Chen, V.J.
The functional role of cysteines in isopenicillin N synthase. Correlation of cysteine reactivities toward sulfhydryl reagents with kinetic properties of cysteine mutants
J. Biol. Chem.
266
11779-11788
1991
Acremonium chrysogenum
brenda
Huffman, G.W.; Gesellchen, P.D.; Turner, J.R.; Rothenberger, R.B.; Osborne, H.E.; Miller, F.D.; Chapman, J.L.; Queener, S.W.
Substrate specificity of isopenicillin N synthase
J. Med. Chem.
35
1897-1914
1992
Acremonium chrysogenum, Penicillium chrysogenum
brenda
Tan, D.S.H.; Sim, T.S.
Functional analysis of conserved histidine residues in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis
J. Biol. Chem.
271
889-894
1996
Acremonium chrysogenum
brenda
Roach, P.L.; Clifton, I.J.; Fulop, V.; Harlos, K.; Barton, G.J.; Hajdu, J.; Andersson, I.; Schofield, C.J.; Baldwin, J.E.
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
Nature
375
700-704
1995
Aspergillus nidulans (P05326)
brenda
Durairaj, M.; Leskiw, B.K.; Jensen, S.E.
Genetic and biochemical analysis of the cysteinyl residues of isopenicillin N synthase from Streptomyces clavuligerus
Can. J. Microbiol.
42
870-875
1996
Streptomyces clavuligerus
brenda
Roach, P.L.; Clifton, I.J.; Hensgens, C.M.H.; Shibta, N.; Schofield, C.J.; Hajdu, J.; Baldwin, J.E.
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
Nature
387
827-830
1997
Aspergillus nidulans (P05326)
brenda
Kreisberg-Zakarin, R.; Borovok, I.; Yanko, M.; Aharonowitz, Y.; Cohen, G.
Recent advances in the structure and function of isopenicillin N synthase
Antonie van Leeuwenhoek
75
33-39
1999
Acremonium chrysogenum, Aspergillus nidulans, Aspergillus nidulans (P05326), Streptomyces jumonjinensis
brenda
Loke, P.; Sim, T.S.
Analysis of glutamines in catalysis in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis
Biochem. Biophys. Res. Commun.
252
472-475
1998
Acremonium chrysogenum
brenda
Rowe, C.J.; Shorrock, C.P.; Claridge, T.D.W.; Sutherland, J.D.
Analysis of the conversion of d-(L-alpha-aminoadipoyl)-L-cysteinyl-D-a-aminobutyrate by active-site mutants of Aspergillus nidulans isopenicillin N synthase
Chem. Biol.
5
229-239
1998
Aspergillus nidulans
brenda
Loke, P.; Ng, C.P.; Sim, T.S.
PCR cloning, heterologous expression, and characterization of isopenicillin N synthase from Streptomyces lipmanii NRRL 3584
Can. J. Microbiol.
46
166-170
2000
Streptomyces microflavus, Streptomyces microflavus NRRL 3584
brenda
Dubus, A.; Sami, M.; Brown, T.J.N.; Schofield, C.J.; Baldwin, J.E.; Frere, J.M.
Studies of isopenicillin N synthase enzymatic properties using a continuous spectrophotometric assay
FEBS Lett.
485
142-146
2000
Aspergillus nidulans
brenda
Kreisberg-Zakarin, R.; Borovok, I.; Yanko, M.; Frolow, F.; Aharonowitz, Y.; Cohen, G.
Structure-function studies of the non-heme iron active site of isopenicillin N synthase: some implications for catalysis
Biophys. Chem.
86
109-118
2000
Streptomyces jumonjinensis
brenda
Loke, P.; Sim, T.S.
Site-directed mutagenesis of proline-285 to leucine in Cephalosporium acremonium isopenicillin N-synthase affects catalysis and increases soluble expression at higher temperatures
Z. Naturforsch. C
56
413-415
2001
Acremonium chrysogenum
brenda
Carr, L.G.; Skatrud, P.L.; Scheetz, M.E 2nd.; Queener, S.W.; Ingolia, T.D.
Cloning and expression of the isopenicillin N synthetase from Penicillium chrysogenum
Gene
48
257-266
1986
Penicillium chrysogenum
brenda
Ullan, R.V.; Casqueiro, J.; Banuelos, O.; Fernandez, F.J.; Gutierrez, S.; Martin, J.F.
A novel epimerization system in fungal secondary metabolism involved in the conversion of isopenicillin N into penicillin N in Acremonium chrysogenum
J. Biol. Chem.
277
46216-46225
2002
Acremonium chrysogenum, Acremonium chrysogenum C10 / ATCC 48272
brenda
Long, A.J.; Clifton, I.J.; Roach, P.L.; Baldwin, J.E.; Rutledge, P.J.; Schofield, C.J.
Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine
Biochemistry
44
6619-6628
2005
Aspergillus nidulans (P05326)
brenda
Howard-Jones, A.R.; Elkins, J.M.; Clifton, I.J.; Roach, P.L.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight
Biochemistry
46
4755-4762
2007
Aspergillus nidulans (P05326)
brenda
Daruzzaman, A.; Clifton, I.J.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase
Chembiochem
7
351-358
2006
Aspergillus nidulans (P05326)
brenda
Gidijala, L.; Bovenberg, R.A.; Klaassen, P.; van der Klei, I.J.; Veenhuis, M.; Kiel, J.A.
Production of functionally active Penicillium chrysogenum isopenicillin N synthase in the yeast Hansenula polymorpha
BMC Biotechnol.
8
29
2008
Penicillium chrysogenum
brenda
Brown, C.D.; Neidig, M.L.; Neibergall, M.B.; Lipscomb, J.D.; Solomon, E.I.
VTVH-MCD and DFT studies of thiolate bonding to [FeNO]7/[FeO2]8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in non-heme Fe enzymes
J. Am. Chem. Soc.
129
7427-7438
2007
Streptomyces microflavus
brenda
Lundberg, M.; Siegbahn, P.E.; Morokuma, K.
The mechanism for isopenicillin N synthase from density-functional modeling highlights the similarities with other enzymes in the 2-His-1-carboxylate family
Biochemistry
47
1031-1042
2008
Aspergillus nidulans
brenda
Ge, W.; Clifton, I.J.; Howard-Jones, A.R.; Stok, J.E.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
Structural studies on the reaction of isopenicillin N synthase with a sterically demanding depsipeptide substrate analogue
ChemBioChem
10
2025-2031
2009
Aspergillus nidulans (P05326)
brenda
Ge, W.; Clifton, I.J.; Stok, J.E.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?
J. Am. Chem. Soc.
130
10096-10102
2008
Aspergillus nidulans
brenda
Liras, P.; Demain, A.L.
Enzymology of beta-lactam compounds with cephem structure produced by actinomycete
Methods Enzymol.
458
401-429
2009
Actinomyces sp.
brenda
Brown-Marshall, C.D.; Diebold, A.R.; Solomon, E.I.
Reaction coordinate of isopenicillin N synthase: oxidase versus oxygenase activity
Biochemistry
49
1176-1182
2010
Aspergillus nidulans
brenda
Douma, R.D.; Verheijen, P.J.; de Laat, W.T.; Heijnen, J.J.; van Gulik, W.M.
Dynamic gene expression regulation model for growth and penicillin production in Penicillium chrysogenum
Biotechnol. Bioeng.
106
608-618
2010
Penicillium chrysogenum
brenda
Clifton, I.J.; Ge, W.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
The crystal structure of isopenicillin N synthase with delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine reveals thioether coordination to iron
Arch. Biochem. Biophys.
516
103-107
2011
Aspergillus nidulans (P05326), Aspergillus nidulans ATCC 38163 (P05326)
brenda
Daruzzaman, A.; Clifton, I.J.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
The interaction of isopenicillin N synthase with homologated substrate analogues delta-(L-alpha-aminoadipoyl)-L-homocysteinyl-D-Xaa characterised by protein crystallography
ChemBioChem
14
599-606
2013
Aspergillus nidulans (P05326), Aspergillus nidulans ATCC 38163 (P05326)
brenda
Clifton, I.J.; Ge, W.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.
The crystal structure of an isopenicillin N synthase complex with an ethereal substrate analogue reveals water in the oxygen binding site
FEBS Lett.
587
2705-2709
2013
Aspergillus nidulans (P05326), Aspergillus nidulans ATCC 38163 (P05326)
brenda
Roelofs, D.; Timmermans, M.J.; Hensbergen, P.; van Leeuwen, H.; Koopman, J.; Faddeeva, A.; Suring, W.; de Boer, T.E.; Marien, J.; Boer, R.; Bovenberg, R.; van Straalen, N.M.
A functional isopenicillin N synthase in an animal genome
Mol. Biol. Evol.
30
541-548
2013
Folsomia candida (K9MVH8), Folsomia candida
brenda
McNeill, L.A.; Brown, T.J.N.; Sami, M.; Clifton, I.J.; Burzlaff, N.I.; Claridge, T.D.W.; Adlington, R.M.; Baldwin, J.E.; Rutledge, P.J.; Schofield, C.J.
Terminally truncated isopenicillin N synthase generates a dithioester product evidence for a thioaldehyde intermediate during catalysis and a new mode of reaction for non-heme iron oxidases
Chemistry
23
12815-12824
2017
Aspergillus nidulans (P05326), Aspergillus nidulans ATCC 38163 (P05326)
brenda
Wang, H.; Pan, Y.; Hu, P.; Zhu, Y.; Li, J.; Jiang, X.; Liu, G.
The autophagy-related gene Acatg1 is involved in conidiation and cephalosporin production in Acremonium chrysogenum
Fungal Genet. Biol.
69
65-74
2014
Acremonium chrysogenum, Acremonium chrysogenum 3.3795
brenda
Tamanaha, E.; Zhang, B.; Guo, Y.; Chang, W.C.; Barr, E.W.; Xing, G.; St Clair, J.; Ye, S.; Neese, F.; Bollinger, J.M.; Krebs, C.
Spectroscopic evidence for the Two C-H-cleaving intermediates of Aspergillus nidulans isopenicillin N synthase
J. Am. Chem. Soc.
138
8862-8874
2016
Aspergillus nidulans
brenda
Francis, W.R.; Shaner, N.C.; Christianson, L.M.; Powers, M.L.; Haddock, S.H.
Occurrence of isopenicillin-N-synthase homologs in bioluminescent ctenophores and implications for coelenterazine biosynthesis
PLoS ONE
10
e0128742
2015
Mycolicibacterium phlei, Gordonia rubripertincta, Crassostrea gigas (K1QF46), Acremonium chrysogenum (P05189), Aspergillus nidulans (P05326), Penicillium chrysogenum (P08703), Streptomyces clavuligerus (P10621), Streptomyces microflavus (P12438), Flavobacterium sp. SC 12154 (P16020), Streptomyces jumonjinensis (P18286), Amycolatopsis lactamdurans (P27744), Lysobacter lactamgenus (Q48739), Streptomyces cattleya (Q53932), Streptomyces griseus (Q54243), Mycolicibacterium phlei RIVM601174, Aspergillus nidulans ATCC 38163 (P05326), Streptomyces clavuligerus ATCC 27064 (P10621), Gordonia rubripertincta NBRC 101908
brenda
Kurzatkowski, W.; Staniszewska, M.; Bondaryk, M.; Gebska-Kuczerowska, A.
Compartmentalization in penicillin G biosynthesis by Penicillium chrysogenum PQ-96
Pol. J. Microbiol.
63
399-408
2014
Penicillium chrysogenum, Penicillium chrysogenum PQ-96
brenda