Structure of histone deacetylases: Insights into substrate recognition and catalysis

被引：75

作者：

Marmorstein, R ^{[1
]}

机构：

[1] Univ Penn, Wistar Inst, Philadelphia, PA 19104 USA

[2] Univ Penn, Dept Chem, Philadelphia, PA 19104 USA

来源：

STRUCTURE | 2001年 / 9卷 / 12期

关键词：

D O I：

10.1016/S0969-2126(01)00690-6

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：

Histone deacetylases catalyze the removal of the acetyl moiety from acetyl-lysine within histories to promote gene repression and silencing. These enzymes fall into distinct families based on primary sequence homology and functional properties in vivo. Recent structural studies of histone deacetylases and their homologs from bacteria have provided important insights into the mode of substrate recognition and catalysis by these enzymes.

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页码：1127 / 1133

页数：7

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