Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene
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DOI：
10.1006/jmbi.1999.3255
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发表时间：
1999-12-03
影响因子：
5.6
通讯作者：
Jansonius, JN
中科院分区：
文献类型：
--
作者：
Capitani, G;Hohenester, E;Jansonius, JN
描述了维生素B-6依赖酶1-氨基-环丙烷-1-羧酸(ACC)合成酶的2.4埃晶体结构。这种酶催化乙烯生物合成的关键步骤，乙烯是一种植物激素，负责启动果实成熟和调节许多其他发育过程。ACC合成酶与已被广泛研究的天冬氨酸氨基转移酶有15%的序列同源性，但催化活性完全不同，但总体折叠和活性部位非常相似。新的结构与现有的生化数据一起使比较机理分析能够在很大程度上解释保守和非保守活性中心残基的催化作用。对一个外部乙二胺反应中间体(外部乙二胺与ACC，即与产物)进行了模拟。新结构为合理设计具有广泛农业应用前景的缓蚀剂提供了依据。(C)1999年学术出版社。
The 2.4 Angstrom crystal structure of the vitamin B-6-dependent enzyme 1-amino-cyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications. (C) 1999 Academic Press.