2bz3

From Proteopedia

Revision as of 10:25, 30 October 2007

STRUCTURE OF E. COLI KAS I H298E MUTANT IN COMPLEX WITH C12 FATTY ACID

Overview

Beta-ketoacyl-acyl carrier protein (ACP) synthase enzymes join short, carbon units to construct fatty acyl chains by a three-step Claisen, condensation reaction. The reaction starts with a trans thioesterification, of the acyl primer substrate from ACP to the enzyme. Subsequently, the, donor substrate malonyl-ACP is decarboxylated to form a carbanion, intermediate, which in the third step attacks C1 of the primer substrate, giving rise to an elongated acyl chain. A subgroup of beta-ketoacyl-ACP, synthases, including mitochondrial beta-ketoacyl-ACP synthase, bacterial, plus plastid beta-ketoacyl-ACP synthases I and II, and a domain of human, fatty acid synthase, have a Cys-His-His triad and also a completely, conserved Lys in the active site. To examine the role of these residues in, ... [(full description)]

About this Structure

2BZ3 is a [Single protein] structure of sequence from [Escherichia coli] with NH4, SO4 and DAO as [ligands]. Active as [Beta-ketoacyl-acyl-carrier-protein synthase I], with EC number [2.3.1.41]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases., von Wettstein-Knowles P, Olsen JG, McGuire KA, Henriksen A, FEBS J. 2006 Feb;273(4):695-710. PMID:16441657

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