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Information on EC 1.8.1.14 - CoA-disulfide reductase
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EC Tree
1.8.1.14 CoA-disulfide reductaseIUBMB Comments
A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-gamma-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH , while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes .
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Word Map
- 1.8.1.14
- staphylococcus
- aureus
- coash
- burgdorferi
- horikoshii
- borrelia
- polysulfide
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mallett
- rhodanese
- furiosus
-
claiborne
- anthracis
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spirochetal
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fad-dependent
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fahey
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multiwavelength
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nadph-binding
- persulfide
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nymphs
-
enzootic
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newton
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karplus
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nucleotide-disulfide
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
coadr, coenzyme a-disulfide reductase, coenzyme a disulfide reductase, bb0728, bacoadr, coa disulfide reductase, coenzyme a disulphide reductase, coa-disulfide reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BB0728
CoA-disulfide reductase (NADH)
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-
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CoA-disulfide reductase (NADH2)
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-
-
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CoADR
coenzyme A disulfide reductase
coenzyme A disulphide reductase
coenzyme A-disulfide reductase
EC 1.6.4.10
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formerly
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NADH-dependent coenzyme A disulfide reductase
NADH2:CoA-disulfide oxidoreductase
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-
-
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NADH:CoA-disulfide oxidoreductase
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-
-
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PH0572
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 CoA + NADP+ = CoA-disulfide + NADPH + H+
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-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
-
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reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
CoA:NADP+ oxidoreductase
A flavoprotein. Not identical with EC 1.8.1.6 (cystine reductase), EC 1.8.1.7 (glutathione-disulfide reductase) or EC 1.8.1.13 (bis-gamma-glutamylcystine reductase). The enzyme from the bacterium Staphylococcus aureus has a strong preference for NADPH [3], while the bacterium Bacillus megaterium contains both NADH and NADPH-dependent enzymes [1].
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CAS REGISTRY NUMBER
COMMENTARY
206770-55-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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+
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-
-
?
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
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-
?
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
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-
?
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
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-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the specific activity with CoA-disulfide as an electron acceptor is about 5fold higher than with menadione
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-
?
CoA-disulfide + NADH + H+
2 CoA + NAD+
the specific activity with CoA-disulfide as an electron acceptor is about 5fold higher than with menadione
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-
?
CoA-disulfide + NADH + H+
CoA + NAD+
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Bacillus anthracis CoADR can use either pyridine nucleotide equally well
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-
?
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+
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Bacillus anthracis CoADR can use either pyridine nucleotide equally well
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-
?
CoA-disulfide + NADPH + H+
CoA + NADP+
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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
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-
?
additional information
?
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both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH, no substrate: dephospho-CoA
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?
additional information
?
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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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?
additional information
?
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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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?
additional information
?
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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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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH
NADH
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CoADR exhibits dual specificity with respect to the NAD(P)H substrate
NADH
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH (depending on the oxidizing substrate), indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
NADPH
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both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH
NADPH
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CoADR exhibits dual specificity with respect to the NAD(P)H substrate
NADPH
the enzyme shows a preference for NADPH (10fold lower Km), although it makes efficient use of NADH as well
NADPH
the turnover number of the enzyme with NADPH is roughly 1.5-2 times greater than with NADH (depending on the oxidizing substrate), indicating that the enzyme is able to use either of the reduced pyridine nucleotides in vivo
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
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.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
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
0.057
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADH, mutant enzyme Y65A/Y66A/P67G/H367G
4.4
CoA-disulfide
pH 7.5, 75°C, wild-type enzyme, cosubstrate: NADPH, wild-type enzyme
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9000
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
2.1
methyl methanethiolsulfonate
mutant enzyme Y419F, at 23°C, pH not specified in the publication
82
methyl methanethiolsulfonate
wild type enzyme, at 23°C, pH not specified in the publication
220
methyl methanethiolsulfonate
mutant enzyme Y361F, at 23°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
(E)-2-(methylsulfonyl)ethenyl-CoA
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00004
(E)-2-(phenylsulfonyl)ethenyl-CoA
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00066
alpha,beta-unsaturated vinyl sulfone-CoA ethyl ester
wild type enzyme, at 37°C, pH not specified in the publication
0.00066
ethyl (2E)-prop-2-en-3-CoA-oate
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.0003
methyl vinyl sulfone-CoA
wild type enzyme, at 37°C, pH not specified in the publication
0.00004
phenyl vinyl sulfone-CoA
wild type enzyme, at 37°C, pH not specified in the publication
0.00516
t-butyl (2E)-prop-2-en-3-CoA-oate
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no activity against oxidized glutathione and thioredoxin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
