Nucleotide specificity of pyruvate kinase and phosphoenolpyruvate carboxykinase

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DOIResolve DOI: http://doi.org/10.1016/0005-2744(76)90190-X
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TypeArticle
Journal titleBiochimica et Biophysica Acta (BBA) - Enzymology
ISSN0005-2744
Volume452
Issue2
Pages406412
AbstractVarious analogues of adenosine 5′-diphosphate with modifications in the heterocyclic base residue were tested as substrates of rabbit muscle pyruvate kinase (ATP:pyruvate 2 - 0 - phosphotransferase, EC. 2.7.1.40) and guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase (GTP:oxaloacetate carboxy-lyase (transphosphorylating), EC 4.1.1.32). The significance of different structural elements for the enzyme-substrate interaction is discussed. While pyruvate kinase shows a rather broad specificity for these analogues, phosphoenolpyruvate carboxykinase has a more stringent requirement for nucleotides, the intact keto and NH groups at C6 and N1 of the pyrimidine ring representing essential sites for the phosphoenolpyruvate carboxykinase substrate interaction. The biological significance of the different substrate specificities of pyruvate kinase and phosphoenolpyruvate carboxykinase is discussed as a possible metabolic control factor.
Publication date
PublisherElsevier/North-Holland Biomedical Press
LanguageEnglish
AffiliationNational Research Council Canada
Peer reviewedYes
NPARC number23001280
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Record identifier4f36f79e-5d57-4627-aa60-b8d23162f64b
Record created2017-01-13
Record modified2017-01-13
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