guanosine-diphosphate and guanosine-5--diphosphate-3--monophosphate

guanosine-diphosphate has been researched along with guanosine-5--diphosphate-3--monophosphate* in 2 studies

Other Studies

2 other study(ies) available for guanosine-diphosphate and guanosine-5--diphosphate-3--monophosphate

Article	Year
2.0 A crystal structure of human ARL5-GDP3'P, a novel member of the small GTP-binding proteins. Biochemical and biophysical research communications, 2005, Jul-08, Volume: 332, Issue:3 ARL5 is a member of ARLs, which is widespread in high eukaryotes and homologous between species. But no structure or biological function of this member is reported. We expressed, purified, and resolved the structure of human ARL5 with bound GDP3'P at 2.0 A resolution. A comparison with the known structures of ARFs shows that besides the typical features of ARFs, human ARL5 has specific features of its own. Bacterially expressed human ARL5 contains bound GDP3'P which is seldom seen in other structures. The hydrophobic tail of the introduced detergent Triton X-305 binds at the possible myristoylation site of Gly2, simulating the myristoylated state of N-terminal amphipathic helix in vivo. The structural features of the nucleotide binding motifs and the switch regions prove that ARL5 will undergo the typical GDP/GTP structural cycle as other members of ARLs, which is the basis of their biological functions. Topics: ADP-Ribosylation Factors; Amino Acid Motifs; Binding Sites; Crystallography, X-Ray; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Macromolecular Substances; Models, Molecular; Protein Conformation; Recombinant Proteins; Static Electricity	2005
Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes. Biochimica et biophysica acta, 1981, Nov-05, Volume: 677, Issue:3-4 Unusual guanosine nucleotides guanosine 5'-diphosphate 3'-diphosphate (ppGpp, also known as MSI) and guanosine 5'-diphosphate 3'-monophosphate (ppGp, also known as MSIII) accumulate to high concentrations in wild-type cells of Escherichia coli during amino acid starvation. We reported here that both nucleotides strongly inhibit the activity of enzymes IMP dehydrogenase and adenylosuccinate synthetase, the first enzymes of the guanylate and adenylate biosynthetic pathways. In both cases, ppGP (MSII) is a stronger inhibitor than ppGpp (MSI). On the other hand, these two nucleotides exhibited opposite effects on the activity of phosphoenolpyruvate carboxylase, the enzyme that utilizes phosphoenolpyruvate. At their respective physiological concentrations, the activity of phosphoenolpyruvate carboxylase is activated by ppGpp and inhibited by ppGp. Topics: Adenylosuccinate Synthase; Enzyme Activation; Escherichia coli; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Tetraphosphate; Guanosine Triphosphate; IMP Dehydrogenase; Phosphoenolpyruvate Carboxylase	1981

Article

Year

2.0 A crystal structure of human ARL5-GDP3'P, a novel member of the small GTP-binding proteins.

Biochemical and biophysical research communications, 2005, Jul-08, Volume: 332, Issue:3

ARL5 is a member of ARLs, which is widespread in high eukaryotes and homologous between species. But no structure or biological function of this member is reported. We expressed, purified, and resolved the structure of human ARL5 with bound GDP3'P at 2.0 A resolution. A comparison with the known structures of ARFs shows that besides the typical features of ARFs, human ARL5 has specific features of its own. Bacterially expressed human ARL5 contains bound GDP3'P which is seldom seen in other structures. The hydrophobic tail of the introduced detergent Triton X-305 binds at the possible myristoylation site of Gly2, simulating the myristoylated state of N-terminal amphipathic helix in vivo. The structural features of the nucleotide binding motifs and the switch regions prove that ARL5 will undergo the typical GDP/GTP structural cycle as other members of ARLs, which is the basis of their biological functions.

Topics: ADP-Ribosylation Factors; Amino Acid Motifs; Binding Sites; Crystallography, X-Ray; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Macromolecular Substances; Models, Molecular; Protein Conformation; Recombinant Proteins; Static Electricity

2005

Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes.

Biochimica et biophysica acta, 1981, Nov-05, Volume: 677, Issue:3-4

Unusual guanosine nucleotides guanosine 5'-diphosphate 3'-diphosphate (ppGpp, also known as MSI) and guanosine 5'-diphosphate 3'-monophosphate (ppGp, also known as MSIII) accumulate to high concentrations in wild-type cells of Escherichia coli during amino acid starvation. We reported here that both nucleotides strongly inhibit the activity of enzymes IMP dehydrogenase and adenylosuccinate synthetase, the first enzymes of the guanylate and adenylate biosynthetic pathways. In both cases, ppGP (MSII) is a stronger inhibitor than ppGpp (MSI). On the other hand, these two nucleotides exhibited opposite effects on the activity of phosphoenolpyruvate carboxylase, the enzyme that utilizes phosphoenolpyruvate. At their respective physiological concentrations, the activity of phosphoenolpyruvate carboxylase is activated by ppGpp and inhibited by ppGp.

Topics: Adenylosuccinate Synthase; Enzyme Activation; Escherichia coli; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Tetraphosphate; Guanosine Triphosphate; IMP Dehydrogenase; Phosphoenolpyruvate Carboxylase

1981