Information on EC 1.2.1.25 - 2-oxoisovalerate dehydrogenase (acylating)

for references in articles please use BRENDA:EC1.2.1.25
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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.2.1.25
-
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RECOMMENDED NAME
GeneOntology No.
2-oxoisovalerate dehydrogenase (acylating)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
oxidative decarboxylation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-isoleucine degradation I
-
-
L-leucine degradation I
-
-
L-valine degradation I
-
-
valine metabolism
-
-
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SYSTEMATIC NAME
IUBMB Comments
3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methyl-propanoylating)
Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.
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CAS REGISTRY NUMBER
COMMENTARY hide
37211-61-3
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH
show the reaction diagram
-
specific for the L-isomer
-
?
4-methyl-2-oxopentanoate + CoA + NAD+
3-methyl-butanoyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
-
required
NAD+
-
required
additional information
-
CoA and NAD+ can be replaced by potassium ferricyanide but the activity is much lower; enzyme probably identical with EC 1.2.4.4
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-oxoisopentanoate
-
competitive
iodoacetate
-
-
L-2-Oxo-3-methylpentanoate
-
competitive
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
CoA
-
-
1.66
L-alpha-keto-beta-methylvalerate
-
-
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
pH 6.0: about 25% of maximal activity, pH 7.5: about 45% of maximal activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Lactococci produce acetic and propionic acid during logarithmic growth and starvation
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.25)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)