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.
Related ArticlesTransition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis.J Mol Biol. 2006
Transition-state complex of the purine-specific nucleoside hydrolase of T. vivax: enzyme conformational changes and implications for catalysis.
Versées W, Barlow J, Steyaert J. J Mol Biol. 2006 Jun 2; 359(2):331-46. Epub 2006 Mar 29.
Leaving group activation by aromatic stacking: an alternative to general acid catalysis.J Mol Biol. 2004
Leaving group activation by aromatic stacking: an alternative to general acid catalysis.
Versées W, Loverix S, Vandemeulebroucke A, Geerlings P, Steyaert J. J Mol Biol. 2004 Apr 16; 338(1):1-6.
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Iminoribitol transition state analogue inhibitors of protozoan nucleoside hydrolases.
Miles RW, Tyler PC, Evans GB, Furneaux RH, Parkin DW, Schramm VL. Biochemistry. 1999 Oct 5; 38(40):13147-54.
Review Enzymatic transition states and transition state analogues.Curr Opin Struct Biol. 2005
Review Enzymatic transition states and transition state analogues.
Schramm VL. Curr Opin Struct Biol. 2005 Dec; 15(6):604-13. Epub 2005 Nov 4.
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Review Atomic motion in enzymatic reaction coordinates.
Schramm VL, Shi W. Curr Opin Struct Biol. 2001 Dec; 11(6):657-65.
The HopQ1 Effector's Nucleoside Hydrolase-Like Domain Is Required for Bacterial Virulence in Arabidopsis and Tomato, but Not Host Recognition in Tobacco.PLoS One. 2013
The HopQ1 Effector's Nucleoside Hydrolase-Like Domain Is Required for Bacterial Virulence in Arabidopsis and Tomato, but Not Host Recognition in Tobacco.
Li W, Chiang YH, Coaker G. PLoS One. 2013; 8(3):e59684. Epub 2013 Mar 26.
Arabidopsis thaliana nucleosidase mutants provide new insights into nucleoside degradation.New Phytol. 2011
Arabidopsis thaliana nucleosidase mutants provide new insights into nucleoside degradation.
Riegler H, Geserick C, Zrenner R. New Phytol. 2011 Jul; 191(2):349-59. Epub 2011 May 20.
Active site plasticity revealed from the structure of the enterobacterial N-ribohydrolase RihA bound to a competitive inhibitor.BMC Struct Biol. 2010
Active site plasticity revealed from the structure of the enterobacterial N-ribohydrolase RihA bound to a competitive inhibitor.
Garau G, Muzzolini L, Tornaghi P, Degano M. BMC Struct Biol. 2010 Jun 8; 10:14. Epub 2010 Jun 8.
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