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dc.contributor.authorSarawut Jitrapakdeeen_US
dc.contributor.authorJohn C. Wallaceen_US
dc.contributor.otherUniversity of Adelaideen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-09-07T08:48:21Z-
dc.date.available2018-09-07T08:48:21Z-
dc.date.issued1999-05-15en_US
dc.identifier.citationBiochemical Journal. Vol.340, No.1 (1999), 1-16en_US
dc.identifier.issn02646021en_US
dc.identifier.other2-s2.0-0033563213en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0033563213&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/25340-
dc.description.abstractPyruvate carboxylase (PC; EC 6.4.1.1), a member of the biotin-dependent enzyme family, catalyses the ATP-dependent carboxylation of pyruvate to oxaloacetate. PC has been found in a wide variety of prokaryotes and eukaryotes. In mammals, PC plays a crucial role in gluconeogenesis and lipogenesis, in the biosynthesis of neurotransmitter substances, and in glucose-induced insulin secretion by pancreatic islets. The reaction catalysed by PC and the physical properties of the enzyme have been studied extensively. Although no high-resolution three-dimensional structure has yet been determined by X-ray crystallography, structural studies of PC have been conducted by electron microscopy, by limited proteolysis, and by cloning and sequencing of genes and cDNA encoding the enzyme. Most well characterized forms of active PC consist of four identical subunits arranged in a tetrahedron-like structure. Each subunit contains three functional domains: the biotin carboxylation domain, the transcarboxylation domain and the biotin carboxyl carrier domain. Different physiological conditions, including diabetes, hyperthyroidism, genetic obesity and postnatal development, increase the level of PC expression through transcriptional and translational mechanisms, whereas insulin inhibits PC expression. Glucocorticoids, glucagon and catecholamines cause an increase in PC activity or in the rate of pyruvate carboxylation in the short term. Molecular defects of PC in humans have recently been associated with four point mutations within the structural region of the PC gene, namely Val145→Ala, Arg151→Cys, Ala610→Thr and Met743→Thr.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0033563213&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleStructure, function and regulation of pyruvate carboxylaseen_US
dc.typeReviewen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1042/0264-6021:3400001en_US
Appears in Collections:Scopus 1991-2000

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