Crystal structure analysis of EstA from Arthrobacter sp Rue61a-an insight into catalytic promiscuity

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. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.