1mpx
ALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINEALPHA-AMINO ACID ESTER HYDROLASE LABELED WITH SELENOMETHIONINE
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedalpha-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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