A study of branched‐chain amino acid aminotransferase and isolation of mutations affecting the catabolism of branched‐chain amino acids in Saccharomyces cerevisiae

FEBS Letters

Dickinson, J.Richard¹  Norte, Valia¹ 

[1] School of Pure & Applied Biology, University of Wales College of Cardiff, Cardiff CF1 3TL, UK

关键词: Catabolism;    Branched-chain amino acid;    Aminotransferase;    Mutation;    Saccharomyces cerevisiae;    EMS;    ethylmethane sulphonate;    Branched-chain amino acid aminotransferase l-branched-chain amino acid;    2-oxoglutarate aminotransferase (EC 2.6.1.6);   

DOI  :  10.1016/0014-5793(93)81754-N

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The specific activity of branched-chain amino acid aminotransferase was highest when S. cerevisiae was grown in minimal medium containing a branched-chain amino acid as nitrogen source. Growth in complex media with glycerol or ethanol gave moderately high levels, whereas with glucose and fructose the specific activity was very low. Mutagenesis defined three genes (BAA1 to BAA3) required for branched-chain amino acid catabolism. The baal mutation reduced the specific activity of the aminotransferase, the stationary phase density in YEPD and caused gross morphological disturbance. Branched-chain amino acid aminotransferase is essential for sporulation.

【 授权许可】

Unknown