Co-factor binding confers substrate specificity to xylose reductase from Debaryomyces hansenii.

ABSTRACT: Binding of substrates into the active site, often through complementarity of shapes and charges, is central to the specificity of an enzyme. In many cases, substrate binding induces conformational changes in the active site, promoting specific interactions between them. In contrast, non-substrates either fail to bind or do not induce the requisite conformational changes upon binding and thus no catalysis occurs. In principle, both lock and key and induced-fit binding can provide specific interactions between the substrate and the enzyme. In this study, we present an interesting case where cofactor binding pre-tunes the active site geometry to recognize only the cognate substrates. We illustrate this principle by studying the substrate binding and kinetic properties of Xylose Reductase from

SUBMITTER: Biswas D 

PROVIDER: S-EPMC3458928 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature