Tracing determinants of dual substrate specificity in glycoside hydrolase family 5.

ABSTRACT: Enzymes are traditionally viewed as having exquisite substrate specificity; however, recent evidence supports the notion that many enzymes have evolved activities against a range of substrates. The diversity of activities across glycoside hydrolase family 5 (GH5) suggests that this family of enzymes may contain numerous members with activities on multiple substrates. In this study, we combined structure- and sequence-based phylogenetic analysis with biochemical characterization to survey the prevalence of dual specificity for glucan- and mannan-based substrates in the GH5 family. Examination of amino acid profile differences between the subfamilies led to the identification and subsequent experimental confirmation of an active site motif indicative of dual specificity. The motif enabled us

SUBMITTER: Chen Z 

PROVIDER: S-EPMC3408205 | biostudies-literature | 2012 Jul

REPOSITORIES: biostudies-literature