Results 201 to 210 of about 23,834 (239)
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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 ...
John C. Wallace +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.
Murray R. Young, Michael C. Scrutton
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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.
Murray R. Young, Michael C. Scrutton
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Kinetics of Nucleotide Binding to Pyruvate Carboxylase
Biochemistry, 1995The kinetics of nucleotide binding to pyruvate carboxylase have been studied by measuring the fluorescence changes that occur on the binding and release of FTP and FDP, which are fluorescent formycin analogues of ATP and ADP. The rate constants and equilibrium binding constants for both MgFTP and MgFDP binding to pyruvate carboxylase have been ...
Michael A. Geeves +2 more
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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.
Ghunwa Nakouzi +2 more
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Prenatal diagnosis of pyruvate carboxylase deficiency
Clinica Chimica Acta, 1982Abstract Deficient pyruvate carboxylase activity was found in the amniotic fluid cells obtained from a pregnancy at risk for pyruvate carboxylase deficiency. The results were corroborated by four independent laboratories. The diagnosis was confirmed by the demonstration that pyruvate carboxylase activity was undetectable in all the tissues examined ...
Barry Wolf +5 more
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Pyruvate carboxylase in the yeast pyc mutant
Archives of Biochemistry and Biophysics, 1987Pyruvate carboxylase deficiency was previously reported to be the biochemical lesion in a yeast mutant, designated pyc, which cannot utilize ethanol, acetate, pyruvate, aspartate, or oxaloacetate as the sole carbon source [C. Wills and T. Melham (1985) Arch. Biochem. Biophys. 236, 782-791; C. Wills et al. (1986) Arch. Biochem. Biophys.
Manfred Rohde +3 more
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Prenatal diagnosis of pyruvate carboxylase deficiency
Prenatal Diagnosis, 1985AbstractPrenatal diagnosis of pyruvate carboxylase (PC) deficiency was performed in a family at risk for the acute neonatal form of this disease which manifests secondary citrullinemia. The diagnosis of an affected child was confirmed by enzyme assay and 3H‐biotin labelling of proteins in cultured fetal skin fibroblasts.
Jennifer R. Toone +5 more
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Pyruvate carboxylase in the developing chick embryo
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973Abstract 1. 1. Pyruvate carboxylase in chick embryo tissue homogenates was stabilized and assayed under optimized conditions. Pyruvate carboxylase activity in embryo liver changed slightly between days 9 and 21 of development. 2. 2. Cell fractionation of embryonic liver showed that 93 per cent of the pyruvate carboxylase was particle bound at
D. Hendrick, F. Moller
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The structure and the mechanism of action of pyruvate carboxylase
The International Journal of Biochemistry & Cell Biology, 1995Pyruvate carboxylase plays an important role in intermediary metabolism, catalysing the formation of oxaloacetate from pyruvate and HCO3-, with concomitant ATP cleavage. It thus provides oxaloacetate for gluconeogenesis and replenishing tricarboxylic acid cycle intermediates for fatty acid, amino acid and neurotransmitter synthesis.
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“Pyruvate Carboxylase, Structure and Function”
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,
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