1b8g
From Proteopedia
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1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE
Overview
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.
About this Structure
1B8G is a Single protein structure of sequence from Malus x domestica with PLP as ligand. Active as 1-aminocyclopropane-1-carboxylate synthase, with EC number 4.4.1.14 Full crystallographic information is available from OCA.
Reference
Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene., Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN, J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:10610793
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