1mpx

From Proteopedia

Revision as of 19:41, 24 November 2007

ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE

Overview

alpha-Amino acid ester hydrolases (AEHs) catalyze the hydrolysis and, synthesis of esters and amides with an alpha-amino group. As such, they, can synthesize beta-lactam antibiotics from acyl compounds and beta-lactam, nuclei obtained from the hydrolysis of natural antibiotics. This article, describes the gene sequence and the 1.9-A resolution crystal structure of, the AEH from Xanthomonas citri. The enzyme consists of an, alpha/beta-hydrolase fold domain, a helical cap domain, and a jellyroll, beta-domain. Structural homology was observed to the Rhodococcus cocaine, esterase, indicating that both enzymes belong to the same class of, bacterial hydrolases. Docking of a beta-lactam antibiotic in the active, site explains the substrate specificity, specifically the necessity of an, alpha-amino group on the substrate, and explains the low specificity, toward the beta-lactam nucleus.

About this Structure

1MPX is a Single protein structure of sequence from Xanthomonas citri with CA and GOL as ligands. Active as Alpha-amino-acid esterase, with EC number 3.1.1.43 Full crystallographic information is available from OCA.

Reference

The sequence and crystal structure of the alpha-amino acid ester hydrolase from Xanthomonas citri define a new family of beta-lactam antibiotic acylases., Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW, J Biol Chem. 2003 Jun 20;278(25):23076-84. Epub 2003 Apr 8. PMID:12684501

Page seeded by OCA on Sat Nov 24 21:48:44 2007