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Substrate activation of pyruvate carboxylase by pyruvate
Biochemical and Biophysical Research Communications, 1969Abstract A kinetic analysis of pyruvate carboxylase isolated from sheep liver and using pyruvate as the variable substrate revealed non-Michaelis Menten kinetic. Double reciprocal plots were biphasic and R S values of 222 were obtained. Hill plots prepared from the initial velocity data showed that at low pyruvate concentrations, the slope of the ...
H, Taylor, J, Nielsen, D B, Keech
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Prenatal Diagnosis, 2018
Pyruvate dehydrogenase deficiency (PDHD) and pyruvate carboxylase deficiency (PCD) are diseases with severe neonatal forms, and their low prevalence makes them difficult to diagnose during pregnancy.
C. Egloff +12 more
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Pyruvate dehydrogenase deficiency (PDHD) and pyruvate carboxylase deficiency (PCD) are diseases with severe neonatal forms, and their low prevalence makes them difficult to diagnose during pregnancy.
C. Egloff +12 more
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Yeast pyruvate carboxylase: Gene isolation
Biochemical and Biophysical Research Communications, 1987To improve our understanding of pyruvate carboxylase (PC)(EC 6.4.1.1) structure and the evolution of the biotin-dependent carboxylases we have isolated and sequenced a yeast (Saccharomyces cerevisiae) genomic DNA fragment encoding PC. The identity of the cloned gene was confirmed by comparing the encoded protein with the sequence of a 26 amino acid ...
C P, Morris, F, Lim, J C, Wallace
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Pyruvate Carboxylase Deficiency
1995Pyruvate carboxylase (PC) deficiency is a rare disorder with autosomal recessive inheritance. Generally, two clinical and biochemical phenotypes of isolated PC deficiency can be distinguished. The so-called French phenotype presents in the neonatal period with severe lactic acidemia and is clinically characterized by failure to thrive, anorexia ...
Marjo S. van der Knaap, Jacob Valk
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Pyruvate carboxylase in genetic obesity
American Journal of Physiology-Endocrinology and Metabolism, 1992Immunoblotting and protein microsequencing were used to identify several adipocyte proteins expressed in an obesity-related fashion in the Zucker rat. One of these was a 116-kDa particulate protein (p116). The p116 levels in adipocytes from 5- to 7-wk-old obese Zucker rats were two- to fivefold higher on a per milligram of protein basis than levels in ...
C J, Lynch +7 more
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Pyruvate carboxylase: Affinity labelling of the pyruvate binding site
Biochemical and Biophysical Research Communications, 1975Abstract The active-site-directed reagent, bromopyruvate has been used to covalently label the pyruvate binding site of pyruvate carboxylase (E.C.6.4.1.1.) isolated from sheep liver. Oxalo-acetate proved to be the most effective reaction component in protecting the enzyme against inactivation; pyruvate was less effective although its efficiency was ...
P J, Hudson, D B, Keech, J C, Wallace
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Pyruvate Metabolism and Control: Factors Affecting Pyruvic Carboxylase Activity
Science, 1964Pyruvic carboxylase activated by acetyl coenzyme A is highly active in the mitochondria of rodent liver, and its activity is increased in fasting and alloxan diabetes. In conjunction with acyl carboxylase activated by di- and tricarboxylic acid, it forms a reciprocating control network.
A D, FREEDMAN, L, KOHN
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Disorders of pyruvate carboxylase and the pyruvate dehydrogenase complex
Journal of Inherited Metabolic Disease, 1996SummaryThe most common defect associated with deficiency of the pyruvate dehydrogenase (PDH) complex occurs in the E1 component, specifically due to mutations in the X‐linked E1α gene. Clinical sequelae of these mutations, which range from severe neonatal lactic acidosis to carbohydrate‐sensitive ataxia, can be different in males and females depending ...
B H, Robinson +3 more
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1972
Publisher Summary This chapter discusses the properties and structure of pyruvate carboxylase. Pyruvate carboxylase activity has been detected in most mammalian tissues examined, although high maximal catalytic capacities for this enzyme are confined to the liver, kidney cortex, and adipose tissue.
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Publisher Summary This chapter discusses the properties and structure of pyruvate carboxylase. Pyruvate carboxylase activity has been detected in most mammalian tissues examined, although high maximal catalytic capacities for this enzyme are confined to the liver, kidney cortex, and adipose tissue.
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Assays of Pyruvate Dehydrogenase Complex and Pyruvate Carboxylase Activity
2011Pyruvate dehydrogenase complex (PDC) and pyruvate carboxylase (PC) are mitochondrial enzymes that provide the initial steps of the two main alternatives for pyruvate metabolism: oxidative decarboxylation vs. anaplerotic carboxylation, gluconeogenesis, and glycerogenesis.
Douglas, Kerr +2 more
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