Information on EC 2.6.1.66 - valine-pyruvate transaminase

for references in articles please use BRENDA:EC2.6.1.66
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.66
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RECOMMENDED NAME
GeneOntology No.
valine-pyruvate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-alanine biosynthesis I
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alanine metabolism
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Valine, leucine and isoleucine biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
L-valine:pyruvate aminotransferase
Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
132421-38-6
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73379-50-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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 + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
show the reaction diagram
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
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
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the transamination of ketoisovalerate (KIV) to valine is carried out mainly by the transaminase B enzyme, with the transaminase C enzyme playing a minor role
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?
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
beta-chloro-L-alanine
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DL-alpha-aminobutanoate
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L-alanine
L-Cycloserine
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L-leucine
L-valine
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growing this microorganism in the presence of valine diminishes transaminase C activity but does not repress avtA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
beta-chloro-L-alanine
Brevibacterium flavum
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above 20 mM, pH 8.0, temperature not specified in the publication
80
DL-alpha-aminobutanoate
Brevibacterium flavum
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above 80 mM, pH 8.0, temperature not specified in the publication
4.1
L-Cycloserine
Brevibacterium flavum
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pH 8.0, temperature not specified in the publication
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homology modeling of structure and comparison with alanine transaminases AlaA and AlaC of Escherichia coli. The enzymes shared the same set of residues for binding the phosphate group and pyrimidine ring of the cofactor. Despite a high degree of sequence conservation in the active site, AvtA is thre least effective due to several changes in residues stabilizing the phosphate group and the secong half reaction
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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