Structural highlights
Publication Abstract from PubMed
In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with beta-lactamase fold and the ability to cleave beta-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C beta-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.
Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity.,Wagner UG, DiMaio F, Kolkenbrock S, Fetzner S FEBS Lett. 2014 Apr 2;588(7):1154-60. doi: 10.1016/j.febslet.2014.02.045. Epub, 2014 Mar 5. PMID:24613918[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wagner UG, DiMaio F, Kolkenbrock S, Fetzner S. Crystal structure analysis of EstA from Arthrobacter sp. Rue61a--an insight into catalytic promiscuity. FEBS Lett. 2014 Apr 2;588(7):1154-60. doi: 10.1016/j.febslet.2014.02.045. Epub, 2014 Mar 5. PMID:24613918 doi:http://dx.doi.org/10.1016/j.febslet.2014.02.045
