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2.6.1.19: 4-aminobutyrate-2-oxoglutarate transaminase

This is an abbreviated version!
For detailed information about 4-aminobutyrate-2-oxoglutarate transaminase, go to the full flat file.

Word Map on EC 2.6.1.19

Reaction

4-aminobutanoate
+
2-oxoglutarate
=
succinate semialdehyde
+
L-glutamate

Synonyms

4-aminobutyrate aminotransferase, 4-aminobutyrate transaminase, 4-aminobutyrate-2-ketoglutarate aminotransferase, 4-aminobutyrate-2-oxoglutarate aminotransferase, 4-aminobutyrate-2-oxoglutarate transaminase, 4-aminobutyric acid 2-ketoglutaric acid aminotransferase, 4-aminobutyric acid aminotransferase, ABAT, aminobutyrate aminotransferase, aminobutyrate transaminase, aminotransferase, aminobutyrate, argD, argD6803, argD7002, Atu3000, beta-alanine aminotransferase, beta-alanine transaminase, beta-alanine-oxoglutarate aminotransferase, beta-alanine-oxoglutarate transaminase, bioA, CG010_026395, CgGABA-AT, GABA aminotransferase, GABA transaminase, GABA transferase, GABA-2-oxoglutarate aminotransferase, GABA-2-oxoglutarate transaminase, GABA-alpha-ketoglutarate aminotransferase, GABA-alpha-ketoglutarate transaminase, GABA-alpha-ketoglutaric acid transaminase, GABA-alpha-oxoglutarate aminotransferase, GABA-AT, GABA-oxoglutarate aminotransferase, GABA-oxoglutarate transaminase, GABA-T, GABA-T1, GABA-T2, GABA-T3, GABA-TA, GABA-transaminase, GABA:2-oxoglutarate aminotransferase, GABAT, GabT, gamma-aminobutyrate aminotransaminase, gamma-aminobutyrate aminotransferase, gamma-aminobutyrate transaminase, gamma-aminobutyrate transaminases, gamma-aminobutyrate-alpha-ketoglutarate aminotransferase, gamma-aminobutyrate-alpha-ketoglutarate transaminase, gamma-aminobutyrate: GABA transaminase, gamma-aminobutyrate:alpha-oxoglutarate aminotransferase, gamma-aminobutyric acid aminotransferase, gamma-aminobutyric acid pyruvate transaminase, gamma-aminobutyric acid transaminase, gamma-aminobutyric acid-2-oxoglutarate transaminase, gamma-aminobutyric acid-alpha-ketoglutarate transaminase, gamma-aminobutyric acid-alpha-ketoglutaric acid aminotransferase, gamma-aminobutyric transaminase, gatT, glutamate-succinic semialdehyde transaminase, homotaurine:2-oxoglutarate aminotransferase, MdGABA-T1, MdGABA-T2, More, NCgl0462, NCgl2515, Osl2, pollen-pistil incompatibility 2, Pop2, SkUga1p, slr1022

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.19 4-aminobutyrate-2-oxoglutarate transaminase

Engineering

Engineering on EC 2.6.1.19 - 4-aminobutyrate-2-oxoglutarate transaminase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E211S
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50G
drastic decrease in kcat-value
E211S/I50G/C77K
10fold increase in decarboxylation activity
E211S/I50G/C77R
drastic decrease in kcat-value
E211S/I50H/V80D
10fold increase in decarboxylation activity, change of reaction specificity to that of a decarboxylase
E211S/I50H/V80T
decrease in kcat, decrease in Km-value for 2-oxoglutarate
E211S/I50N/V80D
drastic decrease in kcat-value
E211S/I50N/V80T
drastic decrease in kcat-value
E211S/I50Q/G295Y/V241A
drastic decrease in kcat-value
I50Q
crystallization data, decrease in kcat, increase in Km-values
I50Q/G295Y
decrease in kcat, decrease in Km-value for 2-oxoglutarate
V241A
crystallization data, decrease in kcat, decrease in Km-value for 2-oxoglutarate
C321M
-
no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
C321S
-
no enzymic activity, behaves as monomer even in absence of 2-mercaptoethanol
K357A
-
no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate
K357B
-
no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate
K357N
-
no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate
K357Q
-
no enzymic activity, even not by addition of exogenous pyridoxal 5’-phosphate
L211F
homozygous missense mutation idientified in in a family with encephalomyopathic mitochondrial DNA depletion syndrome
K274A
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
K274H
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein
K274R
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
K274A
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
-
K274R
-
site-directed mutagenesis, the mutant is unable to bind cofactor PLP and is catalytically inactive
-
synthesis
K330R
-
no catalytic activity, no pyridoxal 5'-phosphate covalently linked to protein
additional information