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从L-精氨酸到一氧化氮途径的酶。

Enzymes of the L-arginine to nitric oxide pathway.

作者信息

Stuehr Dennis J

机构信息

Department of Immunology, Lerner Research Institute, Cleveland Clinic, Cleveland, OH 44195, USA.

出版信息

J Nutr. 2004 Oct;134(10 Suppl):2748S-2751S; discussion 2765S-2767S. doi: 10.1093/jn/134.10.2748S.

DOI:10.1093/jn/134.10.2748S
PMID:15465779
Abstract

L-Arginine is the biological precursor of nitric oxide (NO), which serves as an important signal and effector molecule in animals. This review summarizes some structure-function aspects of the mammalian nitric oxide synthases, which are enzymes that catalyze the oxidation of L-arginine to NO and L-citrulline. These include aspects related to: 1) the chemical transformations of L-arginine during enzyme catalysis, 2) binding of L-arginine or its structural analogs to the nitric oxide synthases, and 3) how L-arginine levels may affect product formation by the nitric oxide synthases and how this can be modulated by structural analogs of L-arginine.

摘要

L-精氨酸是一氧化氮(NO)的生物前体,而一氧化氮在动物体内作为重要的信号和效应分子。本综述总结了哺乳动物一氧化氮合酶的一些结构-功能方面,这些酶催化L-精氨酸氧化生成NO和L-瓜氨酸。其中包括与以下方面相关的内容:1)酶催化过程中L-精氨酸的化学转化;2)L-精氨酸或其结构类似物与一氧化氮合酶的结合;3)L-精氨酸水平如何影响一氧化氮合酶的产物形成,以及L-精氨酸的结构类似物如何对其进行调节。

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