Results 151 to 160 of about 27,301 (195)
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“Pyruvate Carboxylase, Structure and Function”
Sub-Cellular Biochemistry, 2017Pyruvate carboxylase is a metabolic enzyme that fuels the tricarboxylic acid cycle with one of its intermediates and also participates in the first step of gluconeogenesis. This large enzyme is multifunctional, and each subunit contains two active sites that catalyze two consecutive reactions that lead to the carboxylation of pyruvate into oxaloacetate,
Mikel Valle
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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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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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Decarboxylation of oxalacetate by pyruvate carboxylase
Biochemistry, 1986The decarboxylation of oxalacetate by pyruvate carboxylase in the absence of ADP and Pi is stimulated 400-fold by the presence of oxamate, which is an inhibitory analogue of pyruvate. The observation of substrate inhibition when either oxamate or oxalacetate is varied at a fixed concentration of the other indicates that both molecules bind at the same ...
P V, Attwood, W W, Cleland
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On the Intracellular Location of Pyruvate Carboxylase
1971Summary The concept of the exclusive location of pyruvate carboxylase in mitochondria is based upon the analysis of a subcellular fraction representing a mixture of fragments, and on the exclusion of a cytoplasmic location of this enzyme. Preferential extraction of pyruvate carboxylase – as compared to glutamate dehydrogenase – with isotonic ...
G, Weiss, B, Ohly, H, Brod, W, Seubert
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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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Regulation of pyruvate carboxylase activity by pyruvate in mice liver
International Journal of Biochemistry, 1979Abstract 1. 1. In order to study in vivo the possible regulatory role of pyruvate concentrations on pyruvate carboxylase activity. fed or 24 hr-fasted mice received various overloads of unlabeled pyruvate. 2. 2. The effect of these overloads on the incorporation of [2- 14 C]pyruvate into blood glucose was studied. 3. 3.
S, Bas, P, Favarger, S, Rous
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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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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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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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