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Literature DB >> 2539374

The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-ras. The stereochemical course of the GTPase reaction.

Abstract

The use of guanosine 5'-O-(gamma-thio)triphosphate as a substrate for p21 c-Ha-ras was established. By using chirally labeled [gamma-17O,18O]guanosine 5'-O-(gamma-thio)triphosphate, the stereochemical course of the GTPase reaction was determined. The analysis shows that the hydrolysis occurs with inversion at the gamma-phosphorus. This shows that the most likely mechanism is a single step, in-line transfer, without a phosphoenzyme or other phosphorylated intermediate.

Entities: Chemical

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Year: 1989 PMID： 2539374

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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Cited

15 in total

1. Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity.

Authors: P Gideon; J John; M Frech; A Lautwein; R Clark; J E Scheffler; A Wittinghofer
Journal: Mol Cell Biol Date: 1992-05 Impact factor: 4.272

2. Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

Authors: C Allin; M R Ahmadian; A Wittinghofer; K Gerwert
Journal: Proc Natl Acad Sci U S A Date: 2001-07-03 Impact factor: 11.205

Review 3. The biochemistry of ras p21.

Authors: R J Grand; D Owen
Journal: Biochem J Date: 1991-11-01 Impact factor: 3.857

The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-ras. The stereochemical course of the GTPase reaction.

1. Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity.

2. Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.

Review 3. The biochemistry of ras p21.

4. Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.

5. Active site comparisons highlight structural similarities between myosin and other P-loop proteins.

6. Kinetic characterization of guanine-nucleotide-induced exocytosis from permeabilized rat mast cells.

7. Biochemical characterization of the essential GTP-binding protein Obg of Bacillus subtilis.

8. Triphosphate structure of guanylate-binding protein 1 and implications for nucleotide binding and GTPase mechanism.

9. Kinetic isotope effects in Ras-catalyzed GTP hydrolysis: evidence for a loose transition state.

10. Phosphorylation site of NtrC, a protein phosphatase whose covalent intermediate activates transcription.