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Article

Transition state structures and the roles of catalytic residues in GAP-facilitated GTPase of Ras as elucidated by (18)O kinetic isotope effects.

Biochemistry - 2 Jun 2009

Du Xinlin, Sprang Stephen R

Abstract excerpt

Ras-catalyzed guanosine 5' triphosphate (GTP) hydrolysis proceeds through a loose transition state as suggested in our previous study of (18)O kinetic isotope effects (KIE) [ Du , X. et al. ( 2004 ) Proc. Natl. Acad. Sci. U.S.A. 101 , 8858 - 8863 ]. To probe the mechanisms of GTPase activation protein (GAP)-facilitated GTP hydrolysis reactions, we measured the (18)O KIEs in GTP hydrolysis catalyzed by Ras in the...

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Identifiers

PMID: 19610677
DOI: 10.1021/bi802359b
PMCID: PMC3862183

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