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STRUCTURE OF BRANCHED CHAIN KETO ACID DEHYDROGENASE

STRUCTURE OF BRANCHED CHAIN KETO ACID DEHYDROGENASE
支链酮酸脱氢酶的结构
批准号：
3227113
负责人：
JOHN R SOKATCH
金额：
$9.48万
依托单位：
UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR
依托单位国家：
美国
项目类别：
财政年份：
1979
资助国家：
美国
项目状态：
已结题
起止时间：
1979-07-01 至 1987-08-31
来源：
https://reporter.nih.gov/project-details/3227113
关键词：
Pseudomonas aminoacid metabolism bacterial genetics biological models branched chain aminoacid cofactor electron microscopy enzyme complex enzyme induction /repression enzyme structure enzyme substrate complex gel electrophoresis gene expression genetic mapping maple syrup urine disease microorganism metabolism molecular weight mutant orphan disease /drug radiotracer stoichiometry

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英文摘要
Branched chain keto dehydrogenase of Pseudomonas putida is an unusual enzyme whose activity is stimulated by L-valine. The enzyme has been purified to a specific activity of 10 units/mg protein. The purified enzyme contains 4 subunis with molecular weights of 49k, 46k, 39k, and 37k. The 49k protein has been isolated and identified as lipoamide dehydrogenase. The objective of the current year will be to isolate and identify the remainding subunits. The transacylase subunit will be identified by its specific labeling with N-ethyl(2,3-14C) maleimide in the presence of 2-ketoisovalerate. The dehydrogenase (E1) subunit will be identified by its reaction with ferricyanide and the release of radioactive carbon dioxide from 2-keto(1-14C) isovalerate.
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