乙酰转移酶
组蛋白乙酰转移酶
计算生物学
古细菌
生物化学
生物
遗传学
超家族
乙酰化
化学
基因
作者
Fred Dyda,David C. Klein,Alison Burgess Hickman
出处
期刊:Annual Review of Biophysics and Biomolecular Structure
[Annual Reviews]
日期:2000-06-01
卷期号:29 (1): 81-103
被引量:393
标识
DOI:10.1146/annurev.biophys.29.1.81
摘要
Hundreds of acetyltransferases exist. All use a common acetyl donor--acetyl coenzyme A--and each exhibits remarkable specificity for acetyl acceptors, which include small molecules and proteins. Analysis of the primary sequences of these enzymes indicates that they can be sorted into several superfamilies. This review covers the three-dimensional structures of members of one of these superfamilies, now referred to in the literature as the GCN5-related N-acetyltransferases (GNAT), reflecting the importance of one functional category, the histone acetyltransferases. Despite the diversity of substrate specificities, members of the GNAT superfamily demonstrate remarkable similarity in protein topology and mode of acetyl coenzyme A binding, likely reflecting a conserved catalytic mechanism.
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