Catalysis by nucleoside hydrolases.

TitleCatalysis by nucleoside hydrolases.
Publication TypeJournal Article
Year of Publication2003
AuthorsVersées, W., and J. Steyaert
JournalCurr Opin Struct Biol
Date Published2003 Dec
KeywordsBinding Sites, Catalysis, Enzyme Activation, N-Glycosyl Hydrolases, Protein Binding, Protein Conformation, Protein Folding, Ribose, Structural Homology, Protein, Structure-Activity Relationship, Substrate Specificity

Nucleoside hydrolases cleave the N-glycosidic bond of ribonucleosides. Because of their vital role in the protozoan purine salvage pathway, nucleoside hydrolases from parasitic protozoa in particular have been studied extensively by X-ray crystallography, kinetic methods and site-directed mutagenesis. An elaborate network of conserved interactions between the metalloenzyme and the ribose enables steric and electrostatic stabilisation of the oxocarbenium-ion-like transition state. Activation of the leaving group by protonation before the formation of the transition state is a recurring catalytic strategy of enzymes that cleave N-glycosidic bonds. However, the mechanisms underlying leaving group activation are still the subject of debate for the nucleoside hydrolases.

Alternate JournalCurr. Opin. Struct. Biol.
PubMed ID14675552
Research group: