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'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE''' | '''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE''' | ||
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[[Category: Kirsch, J F.]] | [[Category: Kirsch, J F.]] | ||
[[Category: Storici, P.]] | [[Category: Storici, P.]] | ||
[[Category: | [[Category: Ethylene biosynthesis]] | ||
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Revision as of 08:12, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 11:12:15 2008
