Affiliation:
1. Botanisches Institut (Pflanzenphysiologie), Universität Karlsruhe, Kaiserstraße 12, D-7500 Karlsruhe, Bundesrepublik Deutschland
Abstract
1) In kinetic studies, mevinolin proved to be a highly specific inhibitor of partially purified yeast HMG-CoA reductase (Ki = 3.5 nᴍ towards HMG-CoA) and of microsomal HMG-CoA reductase from etiolated radish seedlings (Ki = 2.2 nᴍ). At low concentrations of NADPH, the inhibitor counteracts the sigmoidal response of plant HMG-CoA reductase activity towards the cosubstrate. At higher concentrations of NADPH, the inhibition pattern is of non-competitive type.
2) Our results are extensively compared with that obtained by the use of animal tissue and yeast as an enzyme source in order to discuss model systems probably valid to evaluate properties and regulation of plant as well as yeast HMG-CoA reductase
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
26 articles.
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