Decoupled roles for the atypical, bifurcated binding pocket of the ybfF hydrolase

EE Ellis, CT Adkins, NM Galovska, LD Lavis…

Index: Ellis, Elizabeth E.; Adkins, Chinessa T.; Galovska, Natalie M.; Lavis, Luke D.; Johnson, R. Jeremy ChemBioChem, 2013 , vol. 14, # 9 p. 1134 - 1144

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Citation Number: 7

Abstract

Abstract Serine hydrolases have diverse intracellular substrates, biological functions, and structural plasticity, and are thus important for biocatalyst design. Amongst serine hydrolases, the recently described ybfF enzyme family are promising novel biocatalysts with an unusual bifurcated substrate-binding cleft and the ability to recognize commercially relevant substrates. We characterized in detail the substrate selectivity of a novel ybfF ...