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Information on EC 2.6.1.66 - valine-pyruvate transaminase and Organism(s) Escherichia coli and UniProt Accession P09053

for references in articles please use BRENDA:EC2.6.1.66
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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.66 valine-pyruvate transaminase
IUBMB Comments
Different from EC 2.6.1.42, branched-chain-amino-acid-transaminase.
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This record set is specific for:
Escherichia coli
UNIPROT: P09053
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transaminase c, valine-pyruvate transaminase, l-valine:pyruvate aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alanine-valine transaminase
-
-
-
-
aminotransferase, alanine-oxoisovalerate
-
-
-
-
aminotransferase, valine-pyruvate
-
-
-
-
transaminase C
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
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
-
73379-50-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
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
L-alanine + 3-methyl-2-oxobutanoate
L-valine + pyruvate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
L-alanine
L-leucine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team