Information on EC 1.8.1.14 - CoA-disulfide reductase

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

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EC NUMBER
COMMENTARY hide
1.8.1.14
-
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RECOMMENDED NAME
GeneOntology No.
CoA-disulfide reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 CoA + NADP+ = CoA-disulfide + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
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reduction
-
-
-
-
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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].
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CAS REGISTRY NUMBER
COMMENTARY hide
206770-55-0
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
QM
-
-
Manually annotated by BRENDA team
strain bb0728
-
-
Manually annotated by BRENDA team
no activity in Methanocaldococcus jannaschii
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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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
-
-
-
-
?
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
-
-
-
-
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
-
-
-
-
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-2-(methylsulfonyl)ethenyl-CoA
-
competitive inhibition
(E)-2-(phenylsulfonyl)ethenyl-CoA
-
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002 - 0.006
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
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25°C, pH 7.8
0.047 - 0.575
methyl methanethiolsulfonate
0.001 - 0.002
NADH
0.003 - 0.073
NADPH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 27
CoA-disulfide
2.7
CoA-ethyl disulfide
Staphylococcus aureus
-
25°C, pH 7.8
4.3
CoA-methyl disulfide
Staphylococcus aureus
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25°C, pH 7.8
0.95
CoA-sec-butyl disulfide
Staphylococcus aureus
-
25°C, pH 7.8
1.2 - 10.4
methyl methanethiolsulfonate
0.9 - 27
NADH
0.3 - 8.1
NADPH
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9000
CoA-disulfide
Staphylococcus aureus
Q2FIA5
wild type enzyme, at 23°C, pH not specified in the publication
5535
2.1 - 220
methyl methanethiolsulfonate
8140
0.00027
NADH
Bacillus anthracis
-
wild type enzyme, at 25°C
8
0.0093
NADPH
Bacillus anthracis
-
wild type enzyme, at 25°C
5
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
0.38
-
using NADPH, aerobic conditions, at 25°C
16.9
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using NADH, aerobic conditions, at 25°C
26.7
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using NADH, anaerobic conditions, at 25°C
additional information
-
no activity against oxidized glutathione and thioredoxin
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50000
-
SDS-PAGE
51000
2 * 51000, X-ray crystallography
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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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 15°C
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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)
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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
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ENGINEERING
ORGANISM
UNIPROT
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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
-
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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Show AA Sequence (894 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.14)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)