Results 1 to 10 of about 3,076 (182)

Phylogenetic Study of the Evolution of PEP-Carboxykinase [PDF]

Evolutionary Bioinformatics, 2007
Phosphoenolpyruvate carboxykinase (PCK) is the key enzyme to initiate the gluconeogenic pathway in vertebrates, yeast, plants and most bacteria. Nucleotide specificity divided all PCKs into two groups.
Sanjukta Aich, Louis T.J. Delbaere
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Phosphoenolpyruvate Cycling via Mitochondrial Phosphoenolpyruvate Carboxykinase Links Anaplerosis and Mitochondrial GTP with Insulin Secretion [PDF]

Journal of Biological Chemistry, 2009
Pancreatic beta-cells couple the oxidation of glucose to the secretion of insulin. Apart from the canonical K(ATP)-dependent glucose-stimulated insulin secretion (GSIS), there are important K(ATP)-independent mechanisms involving both anaplerosis and mitochondrial GTP (mtGTP).
Romana Stark, Francisco J. Pasquel, Adina F. Turcu, Rebecca L. Pongratz, Michael Roden, Gary W. Cline, Gerald I. Shulman, Richard G. Kibbey   +7 more
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A GTP-dependent Vertebrate-type Phosphoenolpyruvate Carboxykinase from Mycobacterium smegmatis [PDF]

Journal of Biological Chemistry, 2001
This is the first report on a bacterial verterbrate-type GTP-dependent phosphoenolpyruvate carboxykinase (PCK). The pck gene of Mycobacterium smegmatis was cloned. The recombinant PCK was overexpressed in Escherichia coli in a soluble form and with high activity. The purified enzyme was found to be monomeric (72 kDa), thermophilic (optimum temperature,
Biswarup Mukhopadhyay, Edward M. Concar, R. S. Wolfe   +2 more
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Cyclic AMP stabilizes the mRNA for phosphoenolpyruvate carboxykinase (GTP) against degradation.

Journal of Biological Chemistry, 1988
It is now well established that cAMP induces the transcription rate of the gene for phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) and that this induction is dependent on a nucleotide domain located within the promoter-regulatory region of the gene (Short, J. M., Wynshaw-Boris, A., Short, H. P., and Hanson, R. W. (1986) J. Biol. Chem.
Y Hod, Richard W. Hanson
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Overcoming Diabetes-Induced Hyperglycemia through Inhibition of Hepatic Phosphoenolpyruvate Carboxykinase (GTP) with RNAi [PDF]

Molecular Therapy, 2005
Phosphoenolpyruvate carboxykinase (PEPCK; EC 4.1.1.32) is the rate-controlling enzyme in gluconeogenesis. In diabetic individuals, altered rates of gluconeogenesis are responsible for increased hepatic glucose output and sustained hyperglycemia. Liver-specific inhibition of PEPCK has not been assessed to date as a treatment for diabetes.
Alícia G. Gómez-Valadés, Anna Vidal‐Alabró, Maria Molas, Jordi Boada, Jordi Bermúdez, Ramón Bartrons, José C. Perales   +6 more
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Cysteine 288: An essential hyperreactive thiol of cytosolic phosphoenolpyruvate carboxykinase (GTP)

Journal of Biological Chemistry, 1989
Phosphoenolpyruvate carboxykinase from the cytosol of rat liver has 13 cysteines, at least one of which is known to be very reactive and essential for catalytic activity (Carlson, G. M., Colombo, G., and Lardy, H. A. (1978) Biochemistry 17, 5329-5338). In order to identify the essential cysteine, this enzyme was modified with the fluorescent sulfhydryl
Cristina Lewis, Jerome M. Seyer, G M Carlson   +2 more
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Phosphoenolpyruvate carboxykinase and the critical role of cataplerosis in the control of hepatic metabolism [PDF]

Nutrition & Metabolism, 2005
Background The metabolic function of PEPCK-C is not fully understood; deletion of the gene for the enzyme in mice provides an opportunity to fully assess its function. Methods The gene for the cytosolic form of phosphoenolpyruvate carboxykinase (GTP) (EC
Kalhan Satish C, Conlon Ronald A, Lepage David F, Yang Jianqi, Johnson Mark T, Hakimi Parvin, Reshef Lea, Tilghman Shirley M, Hanson Richard W   +8 more
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A cAMP-regulated RNA-binding protein that interacts with phosphoenolpyruvate carboxykinase (GTP) mRNA.

Journal of Biological Chemistry, 1993
Cyclic-AMP stabilizes phosphoenolpyruvate carboxykinase (GTP) (PEPCK) mRNA against degradation. To investigate the mechanism of this effect, RNA mobility shift assays were used to determine the interaction of cellular proteins with specific domains from the mRNA.
Nira Nachaliel, Deepti Jain, Y Hod
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Isolation and characterization of the gene coding for cytosolic phosphoenolpyruvate carboxykinase (GTP) from the rat. [PDF]

Proceedings of the National Academy of Sciences, 1983
The gene for cytosolic phosphoenolpyruvate carboxykinase (GTP) [GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32] from the rat was isolated from a recombinant library containing the rat genome in phage lambda Charon 4A. The isolated clone, lambda PCK1, contains the complete gene for phosphoenolpyruvate carboxykinase and approximately ...
H Yoo-Warren, John E. Monahan, John Short, Helen B. Short, Alan Bruzel, Anthony Wynshaw‐Boris, Herman Meisner, David Samols, Richard W. Hanson   +8 more
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Mechanism of 3-mercaptopicolinic acid inhibition of hepatic phosphoenolpyruvate carboxykinase (GTP).

Journal of Biological Chemistry, 1976
The hypoglycemic agent 3-mercaptopicolinic acid inhibits gluconeogenesis from lactate by isolated, perfused livers from fasted rats and guinea pigs. A 3-mercaptopicolinate concentration of 50 muM caused a sharp decrease in glucose synthesis, with virtually complete inhibition at 100 muM.
Mireille Jomain-Baum, Vern L. Schramm, Richard W. Hanson   +2 more
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