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美伐他汀(MK 803)对微粒体结合的萝卜和部分纯化的酵母HMG-CoA还原酶(EC.1.1.1.34)的抑制机制。

Mechanisms of inhibition by mevinolin (MK 803) of microsome-bound radish and of partially purified yeast HMG-CoA reductase (EC.1.1.1.34).

作者信息

Bach T J, Lichtenthaler H K

出版信息

Z Naturforsch C Biosci. 1983 Mar-Apr;38(3-4):212-9. doi: 10.1515/znc-1983-3-410.

DOI:10.1515/znc-1983-3-410
PMID:6553442
Abstract
  1. In kinetic studies, mevinolin proved to be a highly specific inhibitor of partially purified yeast HMG-CoA reductase (Ki = 3.5 nM towards HMG-CoA) and of microsomal HMG-CoA reductase from etiolated radish seedlings (Ki = 2.2 nM). 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.
摘要
  1. 在动力学研究中,美伐他汀被证明是部分纯化的酵母HMG-CoA还原酶的高度特异性抑制剂(对HMG-CoA的Ki = 3.5 nM)以及来自黄化萝卜幼苗的微粒体HMG-CoA还原酶的高度特异性抑制剂(Ki = 2.2 nM)。在低浓度的NADPH下,该抑制剂可抵消植物HMG-CoA还原酶活性对共底物的S形反应。在较高浓度的NADPH下,抑制模式为非竞争性类型。2) 我们的结果与使用动物组织和酵母作为酶源所获得的结果进行了广泛比较,以便讨论可能适用于评估植物以及酵母HMG-CoA还原酶特性和调节的模型系统。

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Mechanisms of inhibition by mevinolin (MK 803) of microsome-bound radish and of partially purified yeast HMG-CoA reductase (EC.1.1.1.34).美伐他汀(MK 803)对微粒体结合的萝卜和部分纯化的酵母HMG-CoA还原酶(EC.1.1.1.34)的抑制机制。
Z Naturforsch C Biosci. 1983 Mar-Apr;38(3-4):212-9. doi: 10.1515/znc-1983-3-410.
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Eur J Biochem. 1986 Jan 2;154(1):103-11. doi: 10.1111/j.1432-1033.1986.tb09364.x.

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