Substrate binding and catalysis in heme peroxidases

被引：153

作者：

Smith, AT ^{[1
]}

Veitch, NC

机构：

[1] Univ Sussex, Sch Biol Sci, Brighton BN1 9QG, E Sussex, England

[2] Royal Bot Gardens, Jodrell Lab, Richmond TW9 3DS, Surrey, England

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 1998年 / 2卷 / 02期

关键词：

D O I：

10.1016/S1367-5931(98)80069-0

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：

Peroxidase-catalysed reactions are being analysed at an increasingly advanced level of structural and mechanistic sophistication. A significant development in this respect has been the long-anticipated solution of crystal structures for several plant peroxidases and a fungal peroxidase complexed to benzhydroxamic acid. New insights into peroxide binding and catalysis have been obtained through site-directed mutagenesis, a technique also crucial to recent progress in understanding the diversity of substrate interaction sites associated with peroxidases from different sources.

引用

页码：269 / 278

页数：10

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