Catechol oxidase - structure and activity

被引:230
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
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
收藏
页码:677 / 683
页数:7
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