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 ß-lactamase fold and the ability to cleave ß-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 ß-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.