High impact information on ABAT

• The amino acid sequence predicted from the cDNA sequence shows that the precursor of 4-aminobutyrate aminotransferase consists of the mature enzyme of 473 amino acid residues and an amino-terminal segment of 27 amino acids attributed to the signal peptide [1].
• 4-Aminobutyrate aminotransferase is a key enzyme of the 4-aminobutyric acid shunt [1].
• Chemistry of the inactivation of 4-aminobutyrate aminotransferase by the antiepileptic drug vigabatrin [2].
• 4-Aminobutyrate aminotransferase is inactivated by preincubation with iodosobenzoate at pH 7 [3].
• Modified 4-aminobutyrate aminotransferase (containing 1 disulfide bond) catalyzes a half-transamination reaction; but it is unable to react with 2-oxoglutarate to generate the aldimine form of the enzyme [3].

Biological context of ABAT

• 4-Aminobutyrate aminotransferase. The presence of nonequivalent binding sites [4].
• The spectroscopic properties of pyridoxal 5-phosphate and 5-phospho-pyridoxal-aminooxyacetate bound to different sites on the holoenzyme can be used to deduce proximity relationships between the catalytic sites of 4-aminobutyrate aminotransferase [5].
• The kinetics of resolution of the pyridoxamine phosphate form of the enzyme 4-aminobutyrate aminotransferase were monitored by fluorescence spectroscopy [6].
• In vitro phosphorylation of 4-aminobutyrate aminotransferase by cAMP dependent protein kinase [7].

Anatomical context of ABAT

• Mitochondrial 4-aminobutyrate aminotransferase was synthesized in a cell-free reticulocyte lysate using polysomal RNA isolated from pig brain [8].

Associations of ABAT with chemical compounds

• Altogether, these observations are consistent with the concept that inactivation of 4-aminobutyrate aminotransferase by iodosobenzoate proceeds through disulfide bond formation between vicinal cysteinyl residues of the protein [9].
• 4-Aminobutyrate aminotransferase, reaction of P'P2-bis(5'-pyridoxal) diphosphate with lysyl residues connected with catalytic activity [10].
• The analogues 5-phospho-pyridoxal-aminooxyacetate and 4-vinyl-pyridoxal 5-phosphate inhibit reduced 4-aminobutyrate aminotransferase reconstituted with pyridoxal 5-phosphate, but they do not affect the catalytic activity of the holoenzyme [5].
• 4-Aminobutyrate aminotransferase, the reaction of lysine residues connected with enzymatic activity [11].
• Three cysteine-containing tryptic peptides were isolated and sequenced from mitochondrial 4-aminobutyrate aminotransferase using DABIA (4-dimethylaminoazobenzene-4-iodoacetamide) as specific labeling reagent for sulfhydryl groups [12].

Analytical, diagnostic and therapeutic context of ABAT

• 4-Aminobutyrate aminotransferase (EC 2.6.1.19, 4 aminobutyrate:2-oxoglutarate aminotransferase) is cleaved by trypsin, yielding an enzymatically active species which can be separated from the split peptides by gel filtration [13].

References