[胆固醇羟化细胞色素P-450多肽链中四硝基甲烷修饰的酪氨酸残基的定位]

[Localization of tetranitromethane-modified tyrosine residues in the polypeptide chain of cholesterol-hydroxylating cytochrome P-450].

作者信息

Pikuleva I A, Lapko A G, Akhrem A A, Usanov S A, Chashchin V L

出版信息

Bioorg Khim. 1987 Jun;13(6):739-47.

Abstract

As a continuation of earlier structure-function relationship studies on cholesterol-hydroxylating cytochrome P-450 from the adrenal cortex mitochondria, the present study deals with the distribution of tetranitromethane-modified tyrosine residues in the hemeprotein polypeptide chain. Amino acid residues Tyr-24, -46, -50, -93, -94, -199, -246 are shown to be modified with tetranitromethane. Tyr-93, -94 are supposedly involved in the active site formation of cytochrome P-450.

摘要

作为早期对肾上腺皮质线粒体胆固醇羟化细胞色素P - 450结构 - 功能关系研究的延续，本研究探讨了四硝基甲烷修饰的酪氨酸残基在血红素蛋白多肽链中的分布。已证明氨基酸残基Tyr - 24、- 46、- 50、- 93、- 94、- 199、- 246被四硝基甲烷修饰。据推测，Tyr - 93、- 94参与细胞色素P - 450活性位点的形成。

相似文献

1

[Localization of tetranitromethane-modified tyrosine residues in the polypeptide chain of cholesterol-hydroxylating cytochrome P-450].

Bioorg Khim. 1987 Jun;13(6):739-47.

2

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