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Stereochemistry of phosphoenolpyruvate carboxylation catalyzed by phosphoenolpyruvate carboxykinase

Biochemistry, 1986
The stereochemistry of the carboxylation of phosphoenolpyruvate to yield oxalacetate, catalyzed by chicken liver phosphoenolpyruvate carboxykinase and by Ascaris muscle phosphoenolpyruvate carboxykinase, was determined. The substrate (Z)-3-fluorophosphoenolpyruvate was used for the stereochemical analysis.
Seung Hee Hwang, Thomas Nowak
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Inhibition and Allosteric Regulation of Monomeric Phosphoenolpyruvate Carboxykinase by 3-Mercaptopicolinic Acid.

Biochemistry, 2015
For almost 40 years, it has been known that tryptophan metabolites and picolinic acid analogues act as inhibitors of gluconeogenesis. Early studies observed that 3-mercaptopicolinic acid (MPA) was a potent hypoglycemic agent via inhibition of glucose ...
M. Balan   +4 more
semanticscholar   +1 more source

TWO CASES OF PHOSPHOENOLPYRUVATE CARBOXYKINASE DEFICIENCY

Acta Paediatrica, 1976
ABSTRACT. Two children are described who suffered from hypoglycemia and liver impairment. Assays of gluconeogenic enzymes in liver samples taken immediately after death demonstrated a deficiency of phosphoenolpyruvate carboxykinase, a key enzyme of gluconeogenesis.
J. D. Elema   +4 more
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The kinetic mechanism of yeast phosphoenolpyruvate carboxykinase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1993
The 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,
Ana María Jabalquinto, Emilio Cardemil
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Regulation of Gluconeogenesis at Phosphoenolpyruvate Carboxykinase

1984
Publisher 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 ...
Henry A. Lardy, Peter E. Hughes
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Regulation and roles of phosphoenolpyruvate carboxykinase in plants

Archives of Biochemistry and Biophysics, 2003
Phosphoenolpyruvate carboxykinase (PCK) is probably ubiquitous in flowering plants, but is confined to certain cells or tissues. It is regulated by phosphorylation, which renders it less active by altering both its substrate affinities and its sensitivity to regulation by adenylates.
Robert P. Walker, Richard C. Leegood
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Inactivation of phosphoenolpyruvate carboxykinase by acetaldehyde

Biochemical and Biophysical Research Communications, 1976
Abstract 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 activity in human liver

Forensic Science International, 1986
The 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
Gordon F. Vawter   +2 more
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Phosphoenolpyruvate carboxykinase from Fasciola hepatica

International Journal for Parasitology, 1982
Abstract Behm C. A. and Bryant C. 1982. Phosphoenolpyruvate carboxykinase from Fasciola hepatica. International Journal for Parasitology 12 : 271–278. The kinetic properties of a partially purified preparation of phosphoenolpyruvate carboxykinase (PEPCK) from F. hepatica were examined.
Carolyn A. Behm, Christopher Bryant
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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 ...
Jinsong Liu, R. W. Hanson
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