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5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
CoA disulfide + NADH
CoA + NAD+
-
-
-
-
?
CoA disulfide + NADPH
CoA + NADP+
-
-
-
-
?
CoA-disulfide + NAD(P)H + H+
CoA + NAD(P)+
CoA-disulfide + NADH + H+
2 CoA + NAD+
CoA-disulfide + NADH + H+
CoA + NAD+
CoA-disulfide + NADPH + H+
2 CoA + NADP+
CoA-disulfide + NADPH + H+
CoA + NADP+
CoA-ethyl disulfide + NADPH + H+
?
-
-
-
-
?
CoA-methyl disulfide + NADPH + H+
?
-
-
-
-
?
CoA-sec-butyl disulfide + NADPH + H+
?
-
-
-
-
?
menadione + NADH + H+
? + NAD+
methyl methanethiolsulfonate + NAD(P)H + H+
? + NAD(P)+
-
-
-
?
NADH + CoA-disulfide
NAD+ + CoA
additional information
?
-
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
?
5,5'-dithiobis(2-nitrobenzoic acid) + NADH + H+
2-nitro-5-thiobenzoate + NAD+
-
-
-
?
CoA-disulfide + NAD(P)H + H+
CoA + NAD(P)+
-
specific substrate
-
-
?
CoA-disulfide + NAD(P)H + H+
CoA + NAD(P)+
-
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the specific activity with CoA-disulfide as an electron acceptor is about 5fold higher than with menadione
-
-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the specific activity with CoA-disulfide as an electron acceptor is about 5fold higher than with menadione
-
-
?
CoA-disulfide + NADH + H+
CoA + NAD+
-
Bacillus anthracis CoADR can use either pyridine nucleotide equally well
-
-
?
CoA-disulfide + NADH + H+
CoA + NAD+
-
-
-
-
?
CoA-disulfide + NADH + H+
CoA + NAD+
-
-
-
-
?
CoA-disulfide + NADH + H+
CoA + NAD+
-
-
-
-
?
CoA-disulfide + NADH + H+
CoA + NAD+
-
-
-
?
CoA-disulfide + NADPH + H+
2 CoA + NADP+
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
-
-
?
CoA-disulfide + NADPH + H+
2 CoA + NADP+
the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate
-
-
?
CoA-disulfide + NADPH + H+
2 CoA + NADP+
the phCoADR structure has a narrower access channel for CoA substrates, which suggests that this restriction might be responsible for the poor activity toward the bulky CoA disulfide substrate
-
-
?
CoA-disulfide + NADPH + H+
2 CoA + NADP+
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH, indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
Bacillus anthracis CoADR can use either pyridine nucleotide equally well
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
reduction of CoA disulfide occurs through two steps: thiol-disulfide exchange with the active site cysteine, followed by flavin-mediated hydride transfer from NADPH to reduce the cysteine-CoA disulfide bond and regenerate the active site
-
-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
-
-
-
-
?
menadione + NADH + H+
? + NAD+
-
-
-
?
menadione + NADH + H+
? + NAD+
-
-
-
?
NADH + CoA-disulfide
NAD+ + CoA
-
-
-
?
NADH + CoA-disulfide
NAD+ + CoA
-
-
-
?
additional information
?
-
-
both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH, no substrate: dephospho-CoA
-
-
?
additional information
?
-
catalyzes the NAD(P)Hdependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides
-
-
?
additional information
?
-
-
catalyzes the NAD(P)Hdependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides
-
-
?
additional information
?
-
catalyzes the NAD(P)Hdependent reduction of polysulfide, CoA-polysulfides, and CoA persulfide, as well as the reduction of a range of other small persulfides, including TNB and glutathione persulfides
-
-
?
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0.002 - 0.086
CoA-disulfide
0.005
CoA-ethyl disulfide
-
25°C, pH 7.8
0.008
CoA-methyl disulfide
-
25°C, pH 7.8
0.004
CoA-sec-butyl disulfide
-
25°C, pH 7.8
0.047 - 0.575
methyl methanethiolsulfonate
0.002
CoA-disulfide
-
25°C, wild-type enzyme. Cosubstrate: NADH
0.0025
CoA-disulfide
pH 7.5, 42°C
0.003
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
0.006
CoA-disulfide
-
25°C, pH 7.8
0.006
CoA-disulfide
-
25°C, wild-type enzyme, cosubstrate: NADPH
0.0205
CoA-disulfide
pH 8.1, 50°C, cofactor: NADH
0.0286
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, wild-type enzyme
0.052
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme
0.0562
CoA-disulfide
pH 8.1, 50°C, cofactor: NADPH
0.057
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, mutant enzyme Y65A/Y66A/P67G/H367G
0.086
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G
0.047
methyl methanethiolsulfonate
mutant enzyme Y361F, at 23°C, pH not specified in the publication
0.078
methyl methanethiolsulfonate
wild type enzyme, at 23°C, pH not specified in the publication
0.575
methyl methanethiolsulfonate
mutant enzyme Y419F, at 23°C, pH not specified in the publication
0.001
NADH
-
25°C, wild-type enzyme
0.002
NADH
-
wild type enzyme, at 25°C
0.073
NADH
pH 7.5, 75°C, wild-type enzyme
0.075
NADH
pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G
0.003
NADPH
-
25°C, wild-type enzyme
0.006
NADPH
-
wild type enzyme, at 25°C
0.009
NADPH
at 50°C and pH 8.1 in 1 M Tris buffer
0.0164
NADPH
pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G
0.073
NADPH
at 50°C and pH 8.1 in 1 M Tris buffer
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2.7
CoA-ethyl disulfide
-
25°C, pH 7.8
4.3
CoA-methyl disulfide
-
25°C, pH 7.8
0.95
CoA-sec-butyl disulfide
-
25°C, pH 7.8
1.2 - 10.4
methyl methanethiolsulfonate
0.3
CoA-disulfide
-
25°C, mutant enzyme Y25F. Cosubstrate: NADH
1.11
CoA-disulfide
pH 8.1, 50°C, cofactor: NADH
1.5
CoA-disulfide
pH 8.1, 50°C, cofactor: NADPH
1.8
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G
3.17
CoA-disulfide
-
25°C, pH 7.8
4.4
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme
5
CoA-disulfide
-
25°C, mutant enzyme Y367F. Cosubstrate: NADH
5
CoA-disulfide
pH 7.5, 42°C
5.43
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, wild-type enzyme
18.8
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, mutant enzyme Y65A/Y66A/P67G/H367G
27
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
1.2
methyl methanethiolsulfonate
mutant enzyme Y419F, at 23°C, pH not specified in the publication
6.4
methyl methanethiolsulfonate
wild type enzyme, at 23°C, pH not specified in the publication
10.4
methyl methanethiolsulfonate
mutant enzyme Y361F, at 23°C, pH not specified in the publication
0.9
NADH
-
25°C, mutant enzyme Y25F
0.9
NADH
-
mutant enzyme Y425F, at 25°C
2.3
NADH
pH 7.5, 75°C, wild-type enzyme
7
NADH
-
25°C, mutant enzyme Y367F
7
NADH
-
mutant enzyme Y367F, at 25°C
8.1
NADH
pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G
27
NADH
-
25°C, wild-type enzyme
27
NADH
-
wild type enzyme, at 25°C
0.3
NADPH
-
mutant enzyme Y425F, at 25°C
2 - 8
NADPH
-
25°C, wild-type enzyme
2 - 8
NADPH
-
wild type enzyme, at 25°C
5
NADPH
-
mutant enzyme Y367F, at 25°C
5.8
NADPH
pH 7.5, 75°C, wild-type enzyme
7.2
NADPH
at 50°C and pH 8.1 in 1 M Tris buffer
8.1
NADPH
at 50°C and pH 8.1 in 1 M Tris buffer
21.6
NADPH
pH 7.5, 75°C, mutant enzyme Y65A/Y66A/P67G/H367G
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crystal structure at 2.30 A resolution. The structures of the NADH and NADPH complexes at ca. 2.3 A resolution reveal that a loop consisting of residues Glu180-Thr187 becomes ordered and changes conformation on NAD(P)H binding
-
sitting drop vapor diffusion method, using 16-26% 2-methyl-2,4-pentanediol, 0.2 M magnesium acetate, and 0.1 M sodium cacodylate, pH 6.5, at 15°C
-
hanging and sitting drop vapor diffusion method
hanging drop and sitting drop vapor diffusion methods, using 100 mM Tris, pH 8.0, 2-3 M 1,6-hexanediol, and 200 mM MgCl2
sitting drop vapor diffusion method at room temperature
hanging drop vapour diffusion method
sitting drop vapor diffusion method, using 35-37% (w/v) PEG 600, 0.3-0.4 M MgCl2, and 0.1 M HEPES, pH 7.5 (mutants Y361F and Y419F), or 27% (w/v) PEG 600, 0.4 M MgCl2, pH 7.2 (mutant Y361F/Y419F), or 31% (w/v) PEG 600, 0.4 M MgCl2, and 0.1 M HEPES, pH 7.2 (mutant C43S)
crystallization by vapor diffusion. X-ray structure is determined at 2.9 A resolution
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Setlow, B.; Setlow, P.
Levels of acetyl coenzyme A, reduced and oxidized coenzyme A, and coenzyme A in disulfide linkage to protein in dormant germinated spores and growing and sporulating cells of Bacillus megaterium
J. Bacteriol.
132
444-452
1979
Priestia megaterium, Priestia megaterium QM
brenda
Harris, D.R.; Ward, D.E.; Feasel, J.M.; Lancaster, K.M.; Murphy, R.D.; Mallet, T.C.; Crane, E.J., 3rd
Discovery and characterization of a Coenzyme A disulfide reductase from Pyrococcus horikoshii. Implications for this disulfide metabolism of anaerobic hyperthermophiles
FEBS J.
272
1189-1200
2005
Pyrococcus horikoshii
brenda
Mallett, T.C.; Wallen, J.R.; Karplus, P.A.; Sakai, H.; Tsukihara, T.; Claiborne, A.
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution
Biochemistry
45
11278-11289
2006
Staphylococcus aureus (O52582), Staphylococcus aureus
brenda
Hummel, C.S.; Lancaster, K.M.; Crane, E.J.
Determination of coenzyme A levels in Pyrococcus furiosus and other Archaea: implications for a general role for coenzyme A in thermophiles
FEMS Microbiol. Lett.
252
229-234
2005
Pyrococcus furiosus, Saccharolobus solfataricus, Thermococcus litoralis
brenda
Boylan, J.A.; Hummel, C.S.; Benoit, S.; Garcia-Lara, J.; Treglown-Downey, J.; Crane, E.J.; Gherardini, F.C.
Borrelia burgdorferi bb0728 encodes a coenzyme A disulphide reductase whose function suggests a role in intracellular redox and the oxidative stress response
Mol. Microbiol.
59
475-486
2006
Borreliella burgdorferi, Borreliella burgdorferi bb0728
brenda
Wallen, J.R.; Paige, C.; Mallett, T.C.; Karplus, P.A.; Claiborne, A.
Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity
Biochemistry
47
5182-5193
2008
Bacillus anthracis
brenda
Revell, K.D.; Heldreth, B.; Long, T.E.; Jang, S.; Turos, E.
N-Thiolated beta-lactams: Studies on the mode of action and identification of a primary cellular target in Staphylococcus aureus
Bioorg. Med. Chem.
15
2453-2467
2007
Staphylococcus aureus
brenda
van der Westhuyzen, R.; Strauss, E.
Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus
J. Am. Chem. Soc.
132
12853-12855
2010
Staphylococcus aureus
brenda
Case, C.L.; Rodriguez, J.R.; Mukhopadhyay, B.
Characterization of an NADH oxidase of the flavin-dependent disulfide reductase family from Methanocaldococcus jannaschii
Microbiology
155
69-79
2009
no activity in Methanocaldococcus jannaschii
brenda
Wallace, B.D.; Edwards, J.S.; Wallen, J.R.; Moolman, W.J.; van der Westhuyzen, R.; Strauss, E.; Redinbo, M.R.; Claiborne, A.
Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights
Biochemistry
51
7699-7711
2012
Staphylococcus aureus (Q2FIA5), Staphylococcus aureus
brenda
Herwald, S.; Liu, A.Y.; Zhu, B.E.; Sea, K.W.; Lopez, K.M.; Sazinsky, M.H.; Crane, E.J.
Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr): implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus
Biochemistry
52
2764-2773
2013
Pyrococcus horikoshii (O58308), Pyrococcus horikoshii
brenda
Eggers, C.H.; Caimano, M.J.; Malizia, R.A.; Kariu, T.; Cusack, B.; Desrosiers, D.C.; Hazlett, K.R.; Claiborne, A.; Pal, U.; Radolf, J.D.
The coenzyme A disulphide reductase of Borrelia burgdorferi is important for rapid growth throughout the enzootic cycle and essential for infection of the mammalian host
Mol. Microbiol.
82
679-697
2011
Borreliella burgdorferi, Borreliella burgdorferi B31
brenda
Herwald, S.; Liu, A.; Zhu, B.; Sea, K.; Lopez, K.; Sazinsky, M.; Crane, E.
Structure and substrate specificity of the pyrococcal coenzyme A disulfide reductases/polysulfide reductases (CoADR/Psr). Implications for S(0)-based respiration and a sulfur-dependent antioxidant system in Pyrococcus
Biochemistry
52
2764-2773
2013
Pyrococcus horikoshii (O58308), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58308)
brenda
Lencina, A.M.; Koepke, J.; Preu, J.; Muenke, C.; Gennis, R.B.; Michel, H.; Schurig-Briccio, L.A.
Characterization and X-ray structure of the NADH-dependent coenzyme A disulfide reductase from Thermus thermophilus
Biochim. Biophys. Acta Bioenerg.
1860
148080
2019
Thermus thermophilus (Q72HK3), Thermus thermophilus, Thermus thermophilus ATCC BAA-163 (Q72HK3)
brenda
Sea, K.; Lee, J.; To, D.; Chen, B.; Sazinsky, M.H.; Crane, E.J.
A broader active site in Pyrococcus horikoshii CoA disulfide reductase accommodates larger substrates and reveals evidence of subunit asymmetry
FEBS open bio
8
1083-1092
2018
Pyrococcus horikoshii (O58308), Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860 (O58308)
brenda