Overexpression, crystallization and preliminary X-ray crystallographic analysis of D-ribose-5-phosphate isomerase from Clostridium thermocellum.

ABSTRACT: Rare sugars are used for many industrial and medical purposes and are produced by the interconversion between aldoses and ketoses catalyzed by sugar and sugar-phosphate isomerases. Recently, Clostridium thermocellum d-ribose-5-phosphate isomerase (CTRPI), an aldose-ketose isomerase, was cloned in order to synthesize d-allose and its substrate specificity was further characterized for industrial usage. CTRPI has a novel substrate specificity that differs from those of other isomerases, which have broad substrate specificities. CTRPI prefers aldose substrates such as l-talose, d-ribose and d-allose. CTRPI was purified and crystallized in order to determine its three-dimensional structure and thus to elucidate its enzymatic reaction mechanism and understand its substrate specificity. The crys

SUBMITTER: Jung J 

PROVIDER: S-EPMC2777044 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature