Catechol oxidase - structure and activity

被引：226

作者：

Eicken, C ^{[1
]}

Krebs, B

Sacchettini, JC

机构：

[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA

[2] Univ Munster, Inst Anorgan Chem, D-48149 Munster, Germany

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1999年 / 9卷 / 06期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/S0959-440X(99)00029-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Recently determined structures of copper-containing plant catechol oxidase in three different catalytic states have provided new insights into the mechanism of this enzyme and its relationship to other copper type-3 proteins. Moreover, the active site of catechol oxidase has been found to be structurally conserved with the oxygen-binding site of a molluscan hemocyanin.

引用

页码：677 / 683

页数：7

共 31 条

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