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Catalysis by nucleoside hydrolases

Publication Type:

Journal Article

Authors:

Versees,W.; Steyaert,J.

Source:

Current opinion in structural biology, Volume 13, Issue 6, p.731 - 738 (2003)

URL:

PM:14675552

Keywords:

Binding Sites; Catalysis; chemistry; Crystallography; Enzyme Activation; MECHANISM; methods; mutagenesis; N-Glycosyl Hydrolases; Protein Binding; Protein Conformation; Protein Folding; Ribose; Structural Homology; Protein; Structure-Activity Relationship;

Abstract:

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

Notes:

DA - 20031216
IS - 0959-440X (Print)
LA - eng
PT - Journal Article
PT - Review
RN - 50-69-1 (Ribose)
RN - EC 3.2.2.- (N-Glycosyl Hydrolases)
SB - IM