Results 211 to 220 of about 29,850 (257)
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Phosphoenolpyruvate carboxykinase activity in human liver
Forensic Science International, 1986The activity of phosphoenolpyruvate carboxykinase (EC 4.1.1.32) (PEPCK), a rate-limiting gluconeogenic enzyme, was found decreased by others in genetically determined disorders and in Sudden Infant Death Syndrome (SIDS). To understand these findings, we made a systematic study of normal human hepatic PEPCK activities in specimens obtained under various
C A, McGraw, G F, Vawter, G, Hug
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Anilinonaphthalene sulfonate isomers inactivate phosphoenolpyruvate carboxykinase
Biochemical and Biophysical Research Communications, 1982Abstract Studies with anilinonaphthalene sulfonate and related compounds suggest that the remarkable ability of some of these isomers to inactivate phosphoenolpyruvate carboxykinase depends, in part, on their ability to assume a conformation in which the naphthyl and phenyl rings are coplanar.
D L, Nelson, R, Silverstein
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Limited proteolysis ofSaccharomyces cerevisiae phosphoenolpyruvate carboxykinase
Journal of Protein Chemistry, 1993Incubation of Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase with trypsin under native conditions cases a time-dependent loss of activity and the production of protein fragments. Cleavage sites determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and sequence analyses identified protease-sensitive peptide bonds between ...
L, Herrera +3 more
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Regulation of Gluconeogenesis at Phosphoenolpyruvate Carboxykinase
1984Publisher Summary This chapter discusses the regulation of gluconeogenesis at phosphoenolpyruvate carboxykinase. It describes the formation of phosphoenolpyruvate (P-enolpyruvate) from oxalacetate. P-enolpyruvate carboxy-kinase (PEPCK) has only a single known function but it exists in two isozyme forms in two different cellular locations and its ...
H, Lardy, P E, Hughes
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The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase, in the physiological direction, has been determined. Product inhibition using KHCO3 showed competitive inhibition, when both oxalacetate (OAA) and ATP were varied. Phosphoenolpyruvate showed noncompetitive inhibition against OAA, and competitive inhibition with respect to ATP. Conversely,
A M, Jabalquinto, E, Cardemil
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REGULATION OF PHOSPHOENOLPYRUVATE CARBOXYKINASE (GTP) GENE EXPRESSION
Annual Review of Biochemistry, 1997Phosphoenolpyruvate 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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Inactivation of phosphoenolpyruvate carboxykinase by acetaldehyde
Biochemical and Biophysical Research Communications, 1976Abstract Preincubation with acetaldehyde at 37°C inactivates rat liver phosphoenolpyruvate carboxykinase. The inactivation is dependent upon the acetaldehyde concentration and the pH and duration of preincubation, and is prevented but not reversed by glutathione.
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Phosphoenolpyruvate carboxykinase and gluconeogenesis in grape pericarp
Plant Physiology and Biochemistry, 2015Glycolysis from sugars is necessary at all stages of development of grape pericarp, and this raises the question as to why gluconeogenesis from malate occurs. Phosphoenolpyruvate carboxykinase (PEPCK) is required for gluconeogenesis in grape pericarp.
Robert P. Walker a +5 more
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Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription
Molecular and Cellular Biochemistry, 1991Transcription 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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A mitochondrial phosphoenolpyruvate carboxykinase from rat brain
Archives of Biochemistry and Biophysics, 1972Phosphoenolpyruvate carboxykinase from the rat brain has been purified approximately 6000-fold. This purified enzyme was stable at −20 °C for several months. Phosphoenolpyruvate carboxykinase from the rat brain was found to be mitochondrial, in contrast to that in the rat liver where this enzyme was always present in the soluble form.
S C, Cheng, R H, Cheng
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