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Information on EC 1.8.1.14 - CoA-disulfide reductase and Organism(s) Staphylococcus aureus and UniProt Accession Q2FIA5

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EC Tree
     1 Oxidoreductases
         1.8 Acting on a sulfur group of donors
             1.8.1 With NAD+ or NADP+ as acceptor
                1.8.1.14 CoA-disulfide reductase
IUBMB 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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Staphylococcus aureus
UNIPROT: Q2FIA5
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
coadr, coenzyme a-disulfide reductase, coenzyme a disulfide reductase, bb0728, bacoadr, coa disulfide reductase, coenzyme a disulphide reductase, coa-disulfide reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
coenzyme A-disulfide reductase
-
CoA disulfide reductase
-
-
CoA-disulfide reductase (NADH)
-
-
-
-
CoA-disulfide reductase (NADH2)
-
-
-
-
CoADR
coenzyme A disulfide reductase
-
-
coenzyme A-disulfide reductase
-
NADH2:CoA-disulfide oxidoreductase
-
-
-
-
NADH:CoA-disulfide oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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
-
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 + NAD(P)H + H+
CoA + NAD(P)+
show the reaction diagram
-
-
-
?
methyl methanethiolsulfonate + NAD(P)H + H+
? + NAD(P)+
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
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
Cys43-SSCoA redox center
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
alpha,beta-unsaturated vinyl sulfone-CoA ethyl ester
-
methyl vinyl sulfone-CoA
-
phenyl vinyl sulfone-CoA
-
(E)-2-(methylsulfonyl)ethenyl-CoA
-
competitive inhibition
(E)-2-(phenylsulfonyl)ethenyl-CoA
-
competitive inhibition
ethyl (2E)-prop-2-en-3-CoA-oate
-
competitive inhibition
t-butyl (2E)-prop-2-en-3-CoA-oate
-
competitive inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
0.047 - 0.575
methyl methanethiolsulfonate
0.006
CoA-disulfide
-
25°C, pH 7.8
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
-
25°C, pH 7.8
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
27
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
1.2 - 10.4
methyl methanethiolsulfonate
3.17
CoA-disulfide
-
25°C, pH 7.8
2.7
CoA-ethyl disulfide
-
25°C, pH 7.8
4.3
CoA-methyl disulfide
-
25°C, pH 7.8
0.95
CoA-sec-butyl disulfide
-
25°C, pH 7.8
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9000
CoA-disulfide
wild type enzyme, at 23°C, pH not specified in the publication
2.1 - 220
methyl methanethiolsulfonate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00066
alpha,beta-unsaturated vinyl sulfone-CoA ethyl ester
wild type enzyme, at 37°C, pH not specified in the publication
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
0.0003
(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
ethyl (2E)-prop-2-en-3-CoA-oate
-
temperature not specified in the publication, in 20 mM Tris-HCl, pH 7.4
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
2 * 51000, X-ray crystallography
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 51000, X-ray crystallography
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
hanging drop vapour diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation adenosine 2',5'-diphosphate agarose column chromatography, and Ni-NTA column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mallett, T.C.; Wallen, J.R.; Karplus, P.A.; Sakai, H.; Tsukihara, T.; Claiborne, A.
Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution
Biochemistry
45
11278-11289
2006
Staphylococcus aureus (O52582), Staphylococcus aureus
Manually annotated by BRENDA team
Revell, K.D.; Heldreth, B.; Long, T.E.; Jang, S.; Turos, E.
N-Thiolated beta-lactams: Studies on the mode of action and identification of a primary cellular target in Staphylococcus aureus
Bioorg. Med. Chem.
15
2453-2467
2007
Staphylococcus aureus
Manually annotated by BRENDA team
van der Westhuyzen, R.; Strauss, E.
Michael acceptor-containing coenzyme A analogues as inhibitors of the atypical coenzyme A disulfide reductase from Staphylococcus aureus
J. Am. Chem. Soc.
132
12853-12855
2010
Staphylococcus aureus
Manually annotated by BRENDA team
Wallace, B.D.; Edwards, J.S.; Wallen, J.R.; Moolman, W.J.; van der Westhuyzen, R.; Strauss, E.; Redinbo, M.R.; Claiborne, A.
Turnover-dependent covalent inactivation of Staphylococcus aureus coenzyme A-disulfide reductase by coenzyme A-mimetics: mechanistic and structural insights
Biochemistry
51
7699-7711
2012
Staphylococcus aureus (Q2FIA5), Staphylococcus aureus
Manually annotated by BRENDA team