The enzyme, found in many Gram-positive bacteria, participates in the reductive degradation of pyrimidines. In eukaryotes this activity is catalysed by EC 2.6.1.19, 4-aminobutyrate---2-oxoglutarate transaminase.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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SYSTEMATIC NAME
IUBMB Comments
beta-alanine:2-oxoglutarate aminotransferase
The enzyme, found in many Gram-positive bacteria, participates in the reductive degradation of pyrimidines. In eukaryotes this activity is catalysed by EC 2.6.1.19, 4-aminobutyrate---2-oxoglutarate transaminase.
4-aminobutanoate is also accepted as amino donor, reaction of EC 2.6.1.19. No donors: glycine, alanine, taurine, ornithine, spermine, spermidine, putrescine. Very poor acceptors: pyruvate, glyoxylate, oxaloacetate, phenylpyruvate
2-oxoglutaric acid is a favourable amino acceptor. beta-Alanine, gamma-aminobutanoate, and beta-aminoisobutanoate are preferred amino donors, but taurine, alanine, ornithine, spermine, and spermidine are not
enzyme catalyzes transamination of omega-amino acids including taurine and hypotaurine. beta-Alanine and DL-beta-aminoisobutanoate serve as a good amino donors, 2-oxoglutarate is the only amino acceptor, pyruvate and oxalacetate are inactive
enzyme catalyzes transamination of omega-amino acids including taurine and hypotaurine. beta-Alanine and DL-beta-aminoisobutanoate serve as a good amino donors, 2-oxoglutarate is the only amino acceptor, pyruvate and oxalacetate are inactive
4-aminobutanoate is also accepted as amino donor, reaction of EC 2.6.1.19. No donors: glycine, alanine, taurine, ornithine, spermine, spermidine, putrescine. Very poor acceptors: pyruvate, glyoxylate, oxaloacetate, phenylpyruvate
activity in regenerating rat liver is lower than that in control rat liver, activity is low in newborn rat liver and increases about 5fold, reaching the level observed in adult rat liver
while mammals degrade beta-alanine and 4-aminobutanoate with only one enzyme, but in different tissues, Lachancea kluyveri and related yeasts have two different enzymes to apparently distinguish between the two reactions in a single cell
beta-alanine:2-oxoglutarate aminotransferase PydD and NAD(P)H-dependent malonic semialdehyde reductase PydE together convert beta-alanine into 3-hydroxypropionate and generated glutamate, thereby making the second nitrogen from the pyrimidine ring available for assimilation
brain-type 4-aminobutanoate aminotransferase (EC 2.6.1.19) is cleaved to liver-type beta-AlaAT I protein when incubated with fresh mitochondrial extract from rat liver. The endopeptidase responsible for conversion is the 418-1305 peptide of CPS I, i.e. carbamoylphosphate synthetase I
Pyd4 is involved in both beta-alanine and 4-aminobutanoate transamination. Pyd4 preferentially uses beta-alanine as the amino group donor, but can also use 4-aminobutanoate
the liver enzyme transaminates from beta-alanine to 2-oxoglutaric acid, while the brain enzyme transaminates from gamma-aminobutyric acid, reaction of EC 2.6.1.19. beta-Alanine aminotransferase activity in regenerating rat liver is lower than that in control rat liver
the precursor to isoform beta-AlaAT I consists of a liver-type mature enzyme of 466 amino acid residues, with 34 residues attributed to the leader peptide
both beta-AlaAT I and beta-AlaAT II activities in the liver are increased with the level of protein in the diet in accordance with changes in their mRNA levels. The beta-AlaAT I activity in the kidney is increased by protein-free and low-protein diets in relation to changes in its mRNA level. The level of beta-AlaAT II activity in the kidney is slightly decreased by a protein-free diet. Neither beta-AlaAT I nor beta-AlaAT II activities in the kidney are affected by a high-protein diet