Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.1.32 (phosphoenolpyruvate carboxykinase)
 4,204 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Effect of unusual guanosine nucleotides on the activities of some Escherichia coli cellular enzymes. 611 28

Acyclovir diphosphate (acyclo-GDP) is a metabolite of the antiviral drug acyclovir [9-(2-hydroxyethoxymethyl)guanine]. Seven enzymes capable of catalyzing the phosphorylation of GDP and dGDP (nucleoside diphosphate kinase, pyruvate kinase, creatine kinase, phosphoglycerate kinase, succinyl-CoA synthetase, phosphoenolpyruvate carboxykinase and adenylosuccinate synthetase) also catalyzed the phosphorylation of acyclo-GDP. In general, acyclo-GDP had a lower V'max and a higher K'm than either GDP or dGDP. None of these enzymes showed significantly higher rates of phosphorylation with GDP or acyclo-GDP in herpes simplex virus-infected Vero cells as compared to uninfected Vero cells. The contribution of each enzyme to the phosphorylation of acyclo-GDP in vivo was estimated from the kinetic data from the partially purified enzymes, the level of each enzyme in Vero cells, and the physiological concentrations of both substrates and inhibitors. The relative order of estimated rates of acyclo-GDP phosphorylation in Vero cells was phosphoglycerate kinase much greater than pyruvate kinase greater than phosphoenolpyruvate carboxykinase greater than nucleoside diphosphate kinase greater than succinyl-CoA synthetase greater than creatine kinase greater than adenylosuccinate synthetase. The calculated potential for acyclo-GDP phosphorylation by these enzymes was adequate to account for the amounts of acyclo-GTP formed in cell culture.
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PMID:Phosphorylation of acyclovir diphosphate by cellular enzymes. 715 65