How do kinases transfer phosphoryl groups?

被引：138
作者：
Matte, A [1 ]
Tari, LW [1 ]
Delbaere, LTJ [1 ]
机构：
[1] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada
来源：
STRUCTURE WITH FOLDING & DESIGN | 1998年 / 6卷 / 04期
基金：
英国医学研究理事会;
关键词：
D O I：
10.1016/S0969-2126(98)00043-4
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：
Understanding how phosphoryl transfer is accomplished by kinases, a ubiquitous group of enzymes, is central to many biochemical processes. Qualitative analysis of the crystal structures of enzyme-substrate complexes of kinases reveals structural features of these enzymes important to phosphoryl transfer. Recently determined crystal structures which mimic the transition state complex have added new insight into the debate as to whether kinases use associative or dissociative mechanisms of catalysis. (C) Current Biology Ltd ISSN 0969-2126.
引用
收藏
页码：413 / 419
页数：7
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