guanosine-triphosphate and diguanosine-pentaphosphate

guanosine-triphosphate has been researched along with diguanosine-pentaphosphate* in 2 studies

Other Studies

2 other study(ies) available for guanosine-triphosphate and diguanosine-pentaphosphate

Article	Year
The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects. The Journal of biological chemistry, 2017, 08-04, Volume: 292, Issue:31 H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell proliferation, differentiation, and survival, and their mutants occur frequently in human cancers. The G-domain, which catalyzes GTP hydrolysis and mediates downstream signaling, is 95% conserved between the Ras isoforms. Because of their very high sequence identity, biochemical studies done on H-Ras have been considered representative of all three Ras proteins. We show here that this is not a valid assumption. Using enzyme kinetic assays under identical conditions, we observed clear differences between the three isoforms in intrinsic catalysis of GTP by Ras in the absence and presence of the Ras-binding domain (RBD) of the c-Raf kinase protein (Raf-RBD). Given their identical active sites, isoform G-domain differences must be allosteric in origin, due to remote isoform-specific residues that affect conformational states. We present the crystal structure of N-Ras bound to a GTP analogue and interpret the kinetic data in terms of structural features specific for H-, K-, and N-Ras. Topics: Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Dinucleoside Phosphates; Enzyme Stability; GTP Phosphohydrolases; Guanosine Triphosphate; Humans; Isoenzymes; Ligands; Membrane Proteins; Models, Molecular; Peptide Fragments; Point Mutation; Protein Conformation; Protein Interaction Domains and Motifs; Proto-Oncogene Proteins c-raf; Proto-Oncogene Proteins p21(ras); Recombinant Proteins	2017
Presence of diguanosine tri, tetra-, and pentaphosphates in commercial samples of GTP and guanosine 5'-tetraphosphate. Analytical biochemistry, 1988, Volume: 171, Issue:2 Commercial samples of GTP and guanosine 5'-tetraphosphate were analyzed, with or without previous treatment with alkaline phosphatase, by high-pressure liquid chromatography on a Hypersil ODS column. They showed the presence of diguanosine 5',5"'-Pl,Pn-tri, tetra-, and pentaphosphates in varying amounts depending on the sample, but usually in proportions of around 0.3%. Topics: Alkaline Phosphatase; Dinucleoside Phosphates; Drug Contamination; Drug Industry; Guanine Nucleotides; Guanosine Tetraphosphate; Guanosine Triphosphate; Hydrolysis; Liver; Muscles	1988

Article

Year

The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.

The Journal of biological chemistry, 2017, 08-04, Volume: 292, Issue:31

H-Ras, K-Ras, and N-Ras are small GTPases that are important in the control of cell proliferation, differentiation, and survival, and their mutants occur frequently in human cancers. The G-domain, which catalyzes GTP hydrolysis and mediates downstream signaling, is 95% conserved between the Ras isoforms. Because of their very high sequence identity, biochemical studies done on H-Ras have been considered representative of all three Ras proteins. We show here that this is not a valid assumption. Using enzyme kinetic assays under identical conditions, we observed clear differences between the three isoforms in intrinsic catalysis of GTP by Ras in the absence and presence of the Ras-binding domain (RBD) of the c-Raf kinase protein (Raf-RBD). Given their identical active sites, isoform G-domain differences must be allosteric in origin, due to remote isoform-specific residues that affect conformational states. We present the crystal structure of N-Ras bound to a GTP analogue and interpret the kinetic data in terms of structural features specific for H-, K-, and N-Ras.

Topics: Allosteric Regulation; Allosteric Site; Amino Acid Substitution; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Dinucleoside Phosphates; Enzyme Stability; GTP Phosphohydrolases; Guanosine Triphosphate; Humans; Isoenzymes; Ligands; Membrane Proteins; Models, Molecular; Peptide Fragments; Point Mutation; Protein Conformation; Protein Interaction Domains and Motifs; Proto-Oncogene Proteins c-raf; Proto-Oncogene Proteins p21(ras); Recombinant Proteins

2017

Presence of diguanosine tri, tetra-, and pentaphosphates in commercial samples of GTP and guanosine 5'-tetraphosphate.

Analytical biochemistry, 1988, Volume: 171, Issue:2

Commercial samples of GTP and guanosine 5'-tetraphosphate were analyzed, with or without previous treatment with alkaline phosphatase, by high-pressure liquid chromatography on a Hypersil ODS column. They showed the presence of diguanosine 5',5"'-Pl,Pn-tri, tetra-, and pentaphosphates in varying amounts depending on the sample, but usually in proportions of around 0.3%.

Topics: Alkaline Phosphatase; Dinucleoside Phosphates; Drug Contamination; Drug Industry; Guanine Nucleotides; Guanosine Tetraphosphate; Guanosine Triphosphate; Hydrolysis; Liver; Muscles

1988