Purification and properties of 3-hydroxy-3-methylglutaryl coenzyme A reductase from Pseudomonas.
نویسندگان
چکیده
An inducible 3-hydroxy-3-methylglutaryl (HMG) coenzyme A reductase (mevalonate:NADf oxidoreductase (acylatmg CoA), EC 1.1. l.-) has been purified X-fold from soluble extracts of Pseudomonas to an apparently homogeneous state as judged by disc gel electrophoresis. The molecular weight estimated by gel electrophoresis is 2.6 to 2.8 X 105. The pursed enzyme is free of HMG-CoA lyase (3-hydroxy3-methylglutaryl-CoA acetoacetate lyase, EC 4.1.3.4) or HMG-CoA hgdrolase (3-hydroxy-3-methylglutaryl-CoA hydrolase, EC 3.1.2.5) activities, and catalyzes the following reactions:
منابع مشابه
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 245 15 شماره
صفحات -
تاریخ انتشار 1970