|
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.a |
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 |
2018/11/27 10:22 |
|