Characterization of a branched-chain amino-acid aminotransferase fromSchizosaccharomyces pombe
โ Scribed by Eden, Amir; Benvenisty, Nissim
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 163 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0749-503X
No coin nor oath required. For personal study only.
โฆ Synopsis
The Saccharomyces cerevisiae genes for the cytosolic and mitochondrial branched-chain amino-acid aminotransferases (BCAT) were isolated recently. These genes show significant homology to mammalian ECA39, originally isolated as a gene regulated by the c-myc oncogene. We now report the isolation of the Schizosaccharomyces pombe eca39/BCAT gene. The S. pombe protein shows 47-52% identity to other eukaryotic BCAT proteins isolated from S. cerevisiae, nematode, mouse and man. A genetic growth assay for BCAT activity was established using an S. cerevisiae strain disrupted in both BCAT isoenzymes. Consequently, the activity of the S. pombe BCAT was demonstrated by genetic and biochemical means. Possible applications of BCAT-encoding genes as selection markers in yeast transformation are proposed.
๐ SIMILAR VOLUMES
A method for branched-chain amino acid aminotransferase is described which is based on running the reaction in the reverse of the usual direction with glutamate and r\*-ketoisocaproate as substrates. The cY-ketoglutarate generated is reduced with glutamate dehydrogenase and NADH. For sensitivity in
The influence of intravenous infusion of branched-chain amino acids (BCAAs) on brain function in patients with liver cirrhosis and acute hepatic encephalopathy was examined using a double-blind, randomized study design. Five medical centers in France and Sweden participated, and 50 patients were stu