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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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EC Tree
IUBMB Comments Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
The enzyme appears in viruses and cellular organisms
Synonyms
transaminase c, l-valine:pyruvate aminotransferase,
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alanine-valine transaminase
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aminotransferase, alanine-oxoisovalerate
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aminotransferase, valine-pyruvate
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transaminase C
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L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine
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amino group transfer
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L-valine:pyruvate aminotransferase
Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
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3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
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3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
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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
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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r
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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mutations in the gene encoding this enzyme are silent unless they are combined with mutations involved in isoleucine-valine biosynthesis
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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this enzyme deficiency results in conditional isoleucine auxotrophy in the presence of alanine
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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mutations in the gene encoding this enzyme are silent unless they are combined with mutations involved in isoleucine-valine biosynthesis
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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probably involved in alanine biosynthesis, transaminase C is found at reduced levels upon starvation for any one of several amino acids
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r
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3-methyl-2-oxobutanoate + L-glutamate
L-valine + 2-oxoglutarate
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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
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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mutations in the gene encoding this enzyme are silent unless they are combined with mutations involved in isoleucine-valine biosynthesis
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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this enzyme deficiency results in conditional isoleucine auxotrophy in the presence of alanine
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L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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mutations in the gene encoding this enzyme are silent unless they are combined with mutations involved in isoleucine-valine biosynthesis
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r
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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probably involved in alanine biosynthesis, transaminase C is found at reduced levels upon starvation for any one of several amino acids
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r
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beta-chloro-L-alanine
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DL-alpha-aminobutanoate
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L-valine
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growing this microorganism in the presence of valine diminishes transaminase C activity but does not repress avtA
L-alanine
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growing this microorganism in the presence of alanine represses transaminase C activity
L-alanine
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growing this microorganism in the presence of alanine represses the gene encoding transaminase C
L-leucine
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growing this microorganism in the presence of leucine represses transaminase C activity
L-leucine
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growing this microorganism in the presence of leucine represses the gene encoding transaminase C
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20
beta-chloro-L-alanine
Brevibacterium flavum
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above 20 mM, pH 8.0, temperature not specified in the publication
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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
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brenda
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brenda
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brenda
LT2 strains, avtA gene
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brenda
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brenda
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UniProt
brenda
K12, strain W3110
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brenda
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Q8ZL86
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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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
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expression in Escherichia coli
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Falkinham, J.O.
Identification of a mutation affecting an alanine-alpha-ketoisovalerate transaminase activity in Escherichia coli K-12
Mol. Gen. Genet.
176
147-149
1979
Escherichia coli
brenda
Berg, C.M.; Whalen, W.A.; Archambault, L.B.
Role of alanine-valine transaminase in Salmonella typhimurium and analysis of an avtA:Tn5 mutant
J. Bacteriol.
155
1009-1014
1983
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Magnus, J.B.; Hollwedel, D.; Oldiges, M.; Takors, R.
Monitoring and modeling of the reaction dynamics in the valine/leucine synthesis pathway in Corynebacterium glutamicum
Biotechnol. Prog.
22
1071-1083
2006
Corynebacterium glutamicum
brenda
Melkonyan, L.; Avetisova, G.; Hambardzumyan, A.; Chakhalyan, A.; Saghyan, A.
Study of regulation of some key enzymes of L-alanine biosynthesis by Brevibacterium flavum producer strains
Appl. Biochem. Microbiol.
49
120-124
2013
Brevibacterium flavum, Brevibacterium flavum ATCC 14067
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brenda
Pena-Soler, E.; Fernandez, F.J.; Lopez-Estepa, M.; Garces, F.; Richardson, A.J.; Quintana, J.F.; Rudd, K.E.; Coll, M.; Vega, M.C.
Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli
PLoS ONE
9
e102139
2014
Escherichia coli (P09053)
brenda
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