原创力文档characterization of the channel constriction allowing the access of the substrate to the active site of yeast oxidosqualene cyclase通道收缩的特性允许访问的衬底酵母oxidosqualene酸环化酶的活性部位.pdfVIP
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characterization of the channel constriction allowing the access of the substrate to the active site of yeast oxidosqualene cyclase通道收缩的特性允许访问的衬底酵母oxidosqualene酸环化酶的活性部位
Characterization of the Channel Constriction Allowing
the Access of the Substrate to the Active Site of Yeast
Oxidosqualene Cyclase
Simonetta Oliaro-Bosso, Giulia Caron, Silvia Taramino, Giuseppe Ermondi, Franca Viola, Gianni Balliano*
` `
Dipartimento di Scienza e Tecnologia del Farmaco, Facolta di Farmacia, Universita degli Studi di Torino, Turin, Italy
Abstract
In oxidosqualene cyclases (OSCs), an enzyme which has been extensively studied as a target for hypocholesterolemic or
antifungal drugs, a lipophilic channel connects the surface of the protein with the active site cavity. Active site and channel
are separated by a narrow constriction operating as a mobile gate for the substrate passage. In Saccharomyces cerevisiae
OSC, two aminoacidic residues of the channel/constriction apparatus, Ala525 and Glu526, were previously showed as critical
for maintaining the enzyme functionality. In this work sixteen novel mutants, each bearing a substitution at or around the
channel constrictions, were tested for their enzymatic activity. Modelling studies showed that the most functionality-
lowering substitutions deeply alter the H-bond network involving the channel/constriction apparatus. A rotation of Tyr239
is proposed as part of the mechanism permitting the access of the substrate to the active site. The inhibition of OSC by
squalene was used as a tool for understanding whether the residues under study are involved in a pre-catalytic selection
and docking of the substrate oxidosqualene.
Citation: Oliaro-Bosso S, Caron G, Taramino S, Ermondi G, Viola F, et al. (2011) Characterization of the Channel Constriction Allowing the Access of the Substrate
to the Active Site of Yeast Oxidosqualene Cyclase. PLoS ONE 6(7): e22134. doi:10.1371/journal.pone.0022134
Editor: Annalisa Pastore, National Institute fo
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