An iso-random BiBi mechanism for adenylate kinase

被引：52

作者：

Sheng, XR ^{[1
]}

Li, X ^{[1
]}

Pan, XM ^{[1
]}

机构：

[1] Acad Sinica, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1999年 / 274卷 / 32期

关键词：

D O I：

10.1074/jbc.274.32.22238

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：

An iso-random Bi Bi mechanism has been proposed for adenylate kinase. In this mechanism, one of the enzyme forms can bind the substrates MgATP and AMP, whereas the other form can bind the products MgADP and ADP. In a catalytic cycle, the conformational changes of the free enzyme and the ternary complexes are the rate-limiting steps. The AP(5)A inhibition equations derived from this mechanism show theoretically that AP(5)A acts as a competitive inhibitor for the forward reaction and a mixed noncompetitive inhibitor for the backward reaction.

引用

页码：22238 / 22242

页数：5

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