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Promiscuous enantioselective (−)-γ-lactamase activity in the Pseudomonas fluorescens esterase I

AuthorsTorres, Leticia L.; Schließmann, Anna; Schmidt, Marlen; Silva-Martín, Noella; Hermoso, Juan A. ; Berenguer, José ; Bornscheuer, Uwe T.; Hidalgo, Aurelio
KeywordsPseudomonas fluorescens esterase I (PFEI
Enantioselective (−)-γ-lactamase
Issue Date2012
PublisherRoyal Society of Chemistry (UK)
CitationOrganic and Biomolecular Chemistry 10: 3388-3392 (2012)
AbstractA promiscuous but very enantioselective (−)-γ-lactamase activity in the kinetic resolution of the Vince lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) was detected in the Pseudomonas fluorescens esterase I (PFEI). The lactamase activity was increased 200-fold by the introduction of a point mutation and resulted as enantioselective as the Microbacterium sp. enzyme used industrially in this resolution. The structural and mechanistic determinants for the catalytic promiscuity and enantioselectivity were identified by molecular modeling, setting a ground stone to engineer further amidase-related activities from this esterase.
Publisher version (URL)http://dx.doi.org/10.1039/C2OB06887G
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