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

FEBS letters (2014-03-13)
Ulrike Gabriella Wagner, Frank DiMaio, Stephan Kolkenbrock, Susanne Fetzner
ABSTRACT

In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-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 β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven.

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