1.8.1.14: CoA-disulfide reductase
This is an abbreviated version!
For detailed information about CoA-disulfide reductase, go to the full flat file.
Word Map on EC 1.8.1.14
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1.8.1.14
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staphylococcus
-
aureus
-
coash
-
burgdorferi
-
horikoshii
-
borrelia
-
polysulfide
-
mallett
-
rhodanese
-
furiosus
-
claiborne
-
anthracis
-
spirochetal
-
fad-dependent
-
fahey
-
multiwavelength
-
nadph-binding
-
persulfide
-
nymphs
-
enzootic
-
newton
-
karplus
-
nucleotide-disulfide
- 1.8.1.14
- staphylococcus
- aureus
- coash
- burgdorferi
- horikoshii
- borrelia
- polysulfide
-
mallett
- rhodanese
- furiosus
-
claiborne
- anthracis
-
spirochetal
-
fad-dependent
-
fahey
-
multiwavelength
-
nadph-binding
- persulfide
-
nymphs
-
enzootic
-
newton
-
karplus
-
nucleotide-disulfide
Reaction
2 CoA
+
Synonyms
BACoADR, BB0728, CoA disulfide reductase, CoA-disulfide reductase (NADH), CoA-disulfide reductase (NADH2), CoADR, coenzyme A disulfide reductase, coenzyme A disulphide reductase, coenzyme A-disulfide reductase, EC 1.6.4.10, NADH-dependent coenzyme A disulfide reductase, NADH2:CoA-disulfide oxidoreductase, NADH:CoA-disulfide oxidoreductase, PH0572
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1.8.1.14 CoA-disulfide reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.8.1.14 - CoA-disulfide reductase
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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+
-
-
-
?
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 + 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+
-
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
-
-
?
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
-
-
?
