Mechanistic issues in asparagine synthetase catalysis.
Mechanistic issues in asparagine synthetase catalysis.
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DOI：
10.1002/9780470123188.ch5
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Nigel G. J. Richards;S. Schuster
中科院分区：
文献类型：
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作者：
Nigel G. J. Richards;S. Schuster
天冬酰胺的酶促合成是利用来自谷氨酰胺或氨的氮原子的ATP依赖性过程。尽管动力学和机理研究的历史很长，但对于这种看似简单的羧基活化酶，特别是关于酰胺键形成之前的那些步骤，还没有普遍接受的催化机制。本章讨论了与该机制有关的四个问题：（a）参与谷氨酰胺利用和天冬氨酸活化的活性位点的结构组织;（B）天冬酰胺合成酶与其他酰胺基转移酶的关系;（c）ATP用于活化β-羧基的方式;（d）氮转移的详细机制。
The enzymatic synthesis of asparagine is an ATP-dependent process that utilizes the nitrogen atom derived from either glutamine or ammonia. Despite a long history of kinetic and mechanistic investigation, there is no universally accepted catalytic mechanism for this seemingly straightforward carboxyl group activating enzyme, especially as regards those steps immediately preceding amide bond formation. This chapter considers four issues dealing with the mechanism: (a) the structural organization of the active site(s) partaking in glutamine utilization and aspartate activation; (b) the relationship of asparagine synthetase to other amidotransferases; (c) the way in which ATP is used to activate the beta-carboxyl group; and (d) the detailed mechanism by which nitrogen is transferred.