Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/11298
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Type: Journal article
Title: Pyruvate carboxylase
Author: Wallace, J.
Jitrapakdee, S.
Chapman-Smith, A.
Citation: The International Journal of Biochemistry and Cell Biology, 1998; 30(1):1-5
Publisher: PERGAMON-ELSEVIER SCIENCE LTD
Issue Date: 1998
ISSN: 1357-2725
1878-5875
Abstract: Pyruvate carboxylase [EC 6.4.1.1] is a member of the family of biotin-dependent carboxylases and is found widely among eukaryotic tissues and in many prokaryotic species. It catalyses the ATP-dependent carboxylation of pyruvate to form oxaloacetate which may be utilised in the synthesis of glucose, fat, some amino acids or their derivatives and several neurotransmitters. Diabetes and hyperthyroidism increase the level of expression of pyruvate carboxylase in the long term, while its activity in the short term is controlled by the intramitochondrial concentrations of acetyl-CoA and pyruvate. Many details of this enzyme's regulation are yet to be described in molecular terms. However, progress towards this goal and towards understanding the relationship of pyruvate carboxylase structure to its catalytic reaction mechanism, has been enormously enhanced recently by the cloning and sequencing of genes and cDNAs encoding the approximately 130 kDa subunit of this homotetramer. Defects in the expression or biotinylation of pyruvate carboxylase in humans almost invariably results in early death or at best a severely debilitating psychomotor retardation, clearly reflecting the vital role it plays in intermediary metabolism in many tissues including the brain.
Keywords: Pancreas
Brain
Animals
Humans
Pyruvate Carboxylase Deficiency Disease
Diabetes Mellitus
Hyperthyroidism
Pyruvate Carboxylase
DNA, Complementary
RNA, Messenger
Gene Expression Regulation, Enzymologic
Up-Regulation
Amino Acid Sequence
Catalysis
Molecular Weight
Molecular Sequence Data
DOI: 10.1016/S1357-2725(97)00147-7
Appears in Collections:Aurora harvest 2
Biochemistry publications

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