Crystal structure analysis of EstA from Arthrobacter sp. Rue61a – an insight into catalytic promiscuity. Issue 7 (5th March 2014)

• Record Type: Journal Article
• Authors: Wagner, Ulrike Gabriella; DiMaio, Frank; Kolkenbrock, Stephan; Fetzner, Susanne
• Is Part Of: FEBS letters. Volume 588:Issue 7(2014)
• Page Start: 1154
• Page End: 1160
• Publication Date: 2014-03-05
• Subjects: EstAA -- carboxylesterase from Arthrobacter sp. Rue61a -- EstBBg -- carboxylesterase from Burkholderia gladioli -- P99Ec -- class C β-lactamase from Enterobacter cloacae -- EstU1 -- metagenome derived carboxylesterase -- 2NB -- 2-naphthylbutyrate -- PenG -- penicillin G -- Catalytic promiscuity -- Crystal structure -- Esterase -- β-Lactamase -- Steric hindrance; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2014.02.045
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : EstA has a β‐lactamase fold and shows catalytic promiscuity towards β‐lactams. EstA represents a structural link between type VIII esterases and β‐lactamases. The substrate specificity of these lactamase‐fold enzymes is sterically driven.