| Title : 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_2003_J.Biol.Chem_278_23076 |
| Author(s) : Barends TR , Polderman-Tijmes JJ , Jekel PA , Hensgens CM , de Vries EJ , Janssen DB , Dijkstra BW |
| Ref : Journal of Biological Chemistry , 278 :23076 , 2003 |
| Abstract : 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. |
| ESTHER : Barends_2003_J.Biol.Chem_278_23076 |
| PubMedSearch : Barends_2003_J.Biol.Chem_278_23076 |
| PubMedID: 12684501 |
| Gene_locus related to this paper: xanax-GAA |
| Gene_locus related to this paper: xanax-GAA |
Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW (2003)
The sequence and crystal structure of the alpha -amino acid ester hydrolase from Xanthomonas citri define a new family of beta -lactam antibiotic acylases
Journal of Biological Chemistry
278 :23076
Barends TR, Polderman-Tijmes JJ, Jekel PA, Hensgens CM, de Vries EJ, Janssen DB, Dijkstra BW (2003)
Journal of Biological Chemistry
278 :23076