Information on EC 1.8.1.14 - CoA-disulfide reductase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.8.1.14
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RECOMMENDED NAME
GeneOntology No.
CoA-disulfide reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 CoA + NADP+ = CoA-disulfide + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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
BRENDA Link
KEGG Link
MetaCyc Link
non-pathway related
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
206770-55-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
QM
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Manually annotated by BRENDA team
strain bb0728
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Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA disulfide + NADH
CoA + NAD+
show the reaction diagram
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-
-
-
?
CoA disulfide + NADPH
CoA + NADP+
show the reaction diagram
-
-
-
-
?
CoA-disulfide + NAD(P)H + H+
CoA + NAD(P)+
show the reaction diagram
CoA-disulfide + NADH + H+
CoA + NAD+
show the reaction diagram
CoA-disulfide + NADPH + H+
CoA + NADP+
show the reaction diagram
CoA-ethyl disulfide + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
CoA-methyl disulfide + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
CoA-sec-butyl disulfide + NADPH + H+
?
show the reaction diagram
-
-
-
-
?
methyl methanethiolsulfonate + NAD(P)H + H+
? + NAD(P)+
show the reaction diagram
-
-
-
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NADH + CoA-disulfide
NAD+ + CoA
show the reaction diagram
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 SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA-disulfide + NAD(P)H + H+
CoA + NAD(P)+
show the reaction diagram
Q2FIA5
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-
-
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CoA-disulfide + NADH + H+
CoA + NAD+
show the reaction diagram
CoA-disulfide + NADPH + H+
CoA + NADP+
show the reaction diagram
O58308
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-2-(methylsulfonyl)ethenyl-CoA
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competitive inhibition
(E)-2-(phenylsulfonyl)ethenyl-CoA
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competitive inhibition
alpha,beta-unsaturated vinyl sulfone-CoA ethyl ester
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ethyl (2E)-prop-2-en-3-CoA-oate
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competitive inhibition
methyl vinyl sulfone-CoA
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phenyl vinyl sulfone-CoA
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t-butyl (2E)-prop-2-en-3-CoA-oate
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competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.006
CoA-disulfide
0.005
CoA-ethyl disulfide
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25C, pH 7.8
0.008
CoA-methyl disulfide
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25C, pH 7.8
0.004
CoA-sec-butyl disulfide
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25C, pH 7.8
0.047 - 0.575
methyl methanethiolsulfonate
0.001 - 0.002
NADH
0.003 - 0.073
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 27
CoA-disulfide
2.7
CoA-ethyl disulfide
Staphylococcus aureus
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25C, pH 7.8
4.3
CoA-methyl disulfide
Staphylococcus aureus
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25C, pH 7.8
0.95
CoA-sec-butyl disulfide
Staphylococcus aureus
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25C, pH 7.8
1.2 - 10.4
methyl methanethiolsulfonate
0.9 - 27
NADH
0.3 - 8.1
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9000
CoA-disulfide
Staphylococcus aureus
Q2FIA5
wild type enzyme, at 23C, pH not specified in the publication
5535
2.1 - 220
methyl methanethiolsulfonate
8140
0.00027
NADH
Bacillus anthracis
-
wild type enzyme, at 25C
8
0.0093
NADPH
Bacillus anthracis
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wild type enzyme, at 25C
5
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0003
(E)-2-(methylsulfonyl)ethenyl-CoA
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temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00004
(E)-2-(phenylsulfonyl)ethenyl-CoA
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temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
0.00066
alpha,beta-unsaturated vinyl sulfone-CoA ethyl ester
0.0003
methyl vinyl sulfone-CoA
wild type enzyme, at 37C, pH not specified in the publication
0.00004
phenyl vinyl sulfone-CoA
wild type enzyme, at 37C, pH not specified in the publication
0.00516
t-butyl (2E)-prop-2-en-3-CoA-oate
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temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.38
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using NADPH, aerobic conditions, at 25C
16.9
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using NADH, aerobic conditions, at 25C
26.7
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using NADH, anaerobic conditions, at 25C
additional information
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no activity against oxidized glutathione and thioredoxin
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
Staphylococcus aureus (strain USA300)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 15C
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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
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)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Q-Sepharose column chromatography and Ni-NTA column chromatography
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ammonium sulfate precipitation adenosine 2',5'-diphosphate agarose column chromatography, and Ni-NTA column chromatography
Ni-NTA column chromatography
recombinant enzyme
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T7 antibody agarose column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli B834(DE3) cells; expression in Escherichia coli, wild-type and mutant enzymes C42S, and Y367F, Y425F, and Y367/Y425F
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli C41(DE3) cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y367/Y425F
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inactive mutant enzyme
Y367F
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kcat for NADH is 3.9fold lower than wild-type value, kcat for NADPH is 5.6fold lower than wild-type value; the mutant is 18% as active as wild type enzyme
Y367F/Y425F
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inactive
Y425F
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kcat for NADH is 30fold lower than wild-type value, kcat for NADPH is 93fold lower than wild-type value; the mutant is 1% as active as wild type enzyme
C43S
the enzyme has ca. 0.03% activity relative to the wild type enzyme
Y361F
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y361F/Y419F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
Y419F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
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