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黄嘌呤氧化还原酶钼中心与配体的相互作用

The Interaction between Molybdopterin Cofactor of Xanthine Oxidoreductase and Relative Ligands
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摘要 黄嘌呤氧化还原酶是一种分布广泛的核酸代谢调控酶类,过渡金属钼和蝶呤等辅因子构成其主要的催化活性位点.本文根据PDB数据库中现存的晶体结构和国内外学者多年来在此酶的催化过程、抑制机制等方面开展的实验和理论研究,对其钼中心与底物和抑制剂之间的相互作用形式进行了综述。 The xa-nthine oxidoreductase plays an important role in the metabolism of p＇urines.oxidfzing hypoxanth＇ine to xanthine and xanthine to uric acid.The enzyme features active sites composed of a single Mo atome coordinated by one motybdopterin-based ligand.In this paper the interaction models of the molybdopterin and ligands are reviewed according to the experimental and theoretical studies of the reactivity and structures of the xanthine oxidoreductase.
作者 王传铭 张旭东 王栋 谢昆
机构地区 红河学院云南省高校农作物优质高效栽培与安全控制实验室 云南大学生命科学学院
出处 《红河学院学报》 2013年第2期45-51,共7页 Journal of Honghe University
基金 红河学院中青年学术带头人后备人才基金(2010PY0104) 红河学院科研基金项目(项目编号10XJY113)
关键词 黄嘌呤氧化还原酶 抑制剂 底物 钼辅因子 分子模拟 xanthine oxidoreductase inhibitor substrate molybdenum cofactors molecular simulation
分类号 Q7 [生物学—分子生物学]
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参考文献33

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二级参考文献53

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2013年 第2期

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