development of a coupled assay, employing (R)-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as an auxiliary enzyme, to provide accurate and reliable kinetic constants
a fusion protein of AGT with the membrane-penetrating Tat peptide shows subtle active site conformational changes as compared with untagged AGT, but retains a significant transaminase activity. Active Tat-AGT can be successfully delivered to a mammalian cellular model of primary hyperoxaluria type I consisting of chinese hamster ovary cells expressing glycolate oxidase. The intracellular transduced Tat-AGT makes the cells able to detoxify endogenously produced glyoxylate to an extent similar to that of cells stably expressing AGT
heterogeneous BCAT2 gene mutations R170Q and E264K, found in a 25-year-old patient presenting with headache complaints and mild memory impairment for about six years. The two BCAT2 gene mutations result in decreased BCAT2 enzyme activity. After treatment with vitamin B6, the levels of branched chain amino acids, especially valine are remarkably decreased and brain symmetric white matter abnormal signals are improved
levels of branched-chain aminotransferase-1 transcripts are significantly decreased on the polysomes of lymphoblastoid cell lines derived from Diamond-Blackfan anemia patients and translation of BCAT1 protein is especially impaired in cells with small ribosomal protein gene mutations. This effect may be due in part to the unusually long 5'UTR of the BCAT1 transcript
isobutanol and other branched-chain higher alcohols (BCHAs) are promising advanced biofuels derived from the degradation of branched-chain amino acids (BCAAs). The yeast Saccharomyces cerevisiae is a particularly attractive host for the production of BCHAs due to its high tolerance to alcohols and prevalent use in the bioethanol industry. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p)
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme
usage of PsBCAT in a coupled reaction with Bacillus subtilis ornithine aminotransferase (BsOrnAT), applied to synthesize L-tert-leucine and L-norvaline. The reaction mixture contains 0.5 M Tris-HCl buffer, pH 8.5, 0.1 M trimethylpyruvate or 2-oxovalerate, 20 mM sodium glutamate, 80 mM L-ornithine monohydrochloride, 0.02 mM PLP, 0.2 mg PsBCAT, and 0.05 mg BsOrnAT enzyme in a total volume of 5 ml at 30°C
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme
isobutanol and other branched-chain higher alcohols (BCHAs) are promising advanced biofuels derived from the degradation of branched-chain amino acids (BCAAs). The yeast Saccharomyces cerevisiae is a particularly attractive host for the production of BCHAs due to its high tolerance to alcohols and prevalent use in the bioethanol industry. Degradation of BCAAs begins with transamination reactions, catalyzed by branched-chain amino acid transaminases (BCATs) located in the mitochondria (Bat1p) and cytosol (Bat2p)
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme