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Information on EC 1.8.1.14 - CoA-disulfide reductase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58308
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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
-
mallett
- rhodanese
- furiosus
-
claiborne
- anthracis
-
spirochetal
-
fad-dependent
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fahey
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multiwavelength
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nadph-binding
- persulfide
-
nymphs
-
enzootic
-
newton
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karplus
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nucleotide-disulfide
The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
coadr, coenzyme a-disulfide reductase, coenzyme a disulfide reductase, bb0728, bacoadr, coenzyme a disulphide reductase, coa disulfide reductase, coa-disulfide reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CoA-disulfide reductase (NADH)
-
-
-
-
CoA-disulfide reductase (NADH2)
-
-
-
-
NADH2:CoA-disulfide oxidoreductase
-
-
-
-
NADH:CoA-disulfide oxidoreductase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
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-
-
-
reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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].
CAS REGISTRY NUMBER
COMMENTARY
206770-55-0
-
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
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 + 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
-
-
?
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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-
?
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
?
-
-
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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-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH
NADPH
-
both NADPH and NADH are used efficiently, preference for NADPH with Km-value about eightfold lower than for NADH
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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme is not essential for S0 respiration in Pyrococcus but appears to participate in oxidative defense in the presence of elemental sulfur
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y65A/Y66A/P67G/H367G
the structure of the quadruple mutant shows a widened substrate channel, which is supported by a fourfold increase in kcat for the NAD(P)H-dependent reduction of CoA disulfide and enhanced activity toward the substrate at lower temperatures
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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)
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)
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