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Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription

Molecular and Cellular Biochemistry, 1991
Transcription of the gene for phosphoenolpyruvate carboxykinase is regulated by several hormones which control the level of glucose synthesis in vertebrate animals. A 490 bp segment located at the 5' end of the structural gene contains the necessary regulatory elements to account for the pattern of transcriptional regulation characteristic of the ...
J, Liu, R W, Hanson
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REGULATION OF PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP) GENE EXPRESSION

Annual Review of Biochemistry, 1997
Phosphoenolpyruvate carboxykinase (GTP) (EC 4.1.1.32) (PEPCK) is a key enzyme in the synthesis of glucose in the liver and kidney and of glyceride-glycerol in white adipose tissue and the small intestine. The gene for the cytosolic form of PEPCK (PEPCK-C) is acutely regulated by a variety of dietary and hormonal signals, which result in alteration of ...
R W, Hanson, L, Reshef
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Photochemical cross-linking of guanosine 5'-triphosphate to phosphoenolpyruvate carboxykinase (GTP)

Bioconjugate Chemistry, 1992
Mammalian phosphoenolpyruvate carboxykinase (PEPCK) specifically requires a guanosine or inosine nucleotide as a substrate; however, the structural basis for this nucleotide specificity is not yet known. Because affinity labels derived from guanosine have not yielded a stable, modified peptide in quantities sufficient for sequence analysis, we have ...
C T, Lewis, J M, Seyer, G M, Carlson
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Insulin and glucagon regulate cytosolic phosphoenolpyruvate carboxykinase (GTP) mRNA in rat liver

Diabetes, 1984
Insulin causes a 7–10-fold decrease of both the mRNA that codes for rat hepatic phosphoenolpyruvate carboxykinase (mRNAPEPCK) and of PEPCK synthesis, provided the animals are made diabetic and fed chow. mRNAPEPCK, measured either by in vitro translation or cDNA hybridization, decreases with a half-time of 30–60 min after insulin treatment.
E, Beale   +4 more
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Cyclic AMP and the synthesis of phosphoenolpyruvate carboxykinase (GTP) mRNA

Trends in Biochemical Sciences, 1983
The regulation of cytosolic phosphoenolpyruvate carboxykinase RNA by cyclic-AMP-dependent hormones is discussed, with special emphasis on transcriptional control in isolated nuclei. A model is proposed to account for stimulation of phosphoenolpyruvate carboxykinase RNA synthesis by cyclic AMP.
Herman Meisner   +2 more
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Purification of Phosphoenolpyruvate Carboxykinase (GTP) by Affinity Chromatography on Agarose-Hydrazide-GTP

Enzyme, 1979
The cytosolic form of phosphoenolpyruvate carboxykinase (GTP; EC 4.1.1.32) from rat liver was purified by a procedure involving affinity chromatography on agarose-hydrazide-GTP. Phosphoenolpyruvate carboxykinase is retained quantitatively by the affinity medium in the presence of manganese and can be specifically eluted by a pulse of GTP.
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A GTP-dependent Phosphoenolpyruvate Carboxykinase from Crassostrea gigas Involved in Immune Recognition

Developmental & Comparative Immunology, 2017
Phosphoenolpyruvate carboxykinase (PEPCK) is well known as a key enzyme involved in the metabolic pathway of gluconeogenesis in organisms, but the information about its involvement in immune response is still very limited. In the present study, a novel PEPCK homolog named CgPEPCK was identified from oyster Crassostrea gigas.
Zhao Lv   +9 more
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Modified 3-Alkyl-1,8-dibenzylxanthines as GTP-Competitive inhibitors of phosphoenolpyruvate carboxykinase

Bioorganic & Medicinal Chemistry Letters, 2003
The first non-substrate like inhibitors of human cytosolic phosphoenolpyruvate carboxykinase (PEPCK) competitive with GTP are reported. An effort to discover orally active compounds that improve glucose homeostasis in Type 2 diabetics by reversibly inhibiting PEPCK led to the discovery of 1-allyl-3-butyl-8-methylxanthine (5).
Louise H, Foley   +5 more
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Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site

Journal of Molecular Biology, 2002
We report crystal structures of the human enzyme phosphoenolpyruvate carboxykinase (PEPCK) with and without bound substrates. These structures are the first to be determined for a GTP-dependent PEPCK, and provide the first view of a novel GTP-binding site unique to the GTP-dependent PEPCK family.
Pete, Dunten   +10 more
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