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B6db references: 10610793

type Journal Article
authors Capitani G.; Hohenester, E.; Feng, L.; Storici, P.; Kirsch, J.F.; Jansonius, J.N.
title Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene
journal J Mol Biol
Activity 4.4.1.14
Family 4.4.1.14
sel selected
ui 10610793
year (1999)
volume 294
number 3
pages 745-56
 
abstract The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-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.
last changed 2009/07/01 14:17

B6db references