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Authordc.contributor.authorCampos Campos, Maritza Pamela 
Authordc.contributor.authorGuixé Leguía, Victoria Cristina 
Authordc.contributor.authorBabul, A. 
Cita de ítemdc.identifier.citationJournal of Biological Chemistry, Volumen 259, Issue 10, 2018, Pages 6147-6152
Abstractdc.description.abstractThe kinetic mechanisms of Escherichia coli phosphofructokinase-2 (Pfk-2) and of the mutant enzyme Pfk-2* were investigated. Initial velocity studies showed that both enzymes have a sequential kinetic mechanism, indicating that both substrates must bind to the enzyme before any products are released. For Pfk-2, the product inhibition kinetics was as follows: fructose-1,6-P2 was a competitive inhibitor versus fructose-6-P at two ATP concentrations (0.1 and 0.4 mM), and noncompetitive versus ATP. The other product inhibition patterns, ADP versus either ATP or fructose-6-P were noncompetitive. Dead-end inhibition studies with an ATP analogue, adenylyl imidodiphosphate, showed uncompetitive inhibition when fructose-6-P was the varied substrate. For Pfk-2!a,, the product inhibition studies revealed that ADP was a competitive inhibitor versus ATP at two fructose-6-Pconcentrations (0.05 and 0.5 mM), and noncompetitive versus fructose-6-P. The other product, fructose-1,6-P2, showed noncompetiti
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.uri
Sourcedc.sourceJournal of Biological Chemistry
Keywordsdc.subjectMolecular Biology
Keywordsdc.subjectCell Biology
Títulodc.titleKinetic mechanism of phosphofructokinase-2 from Escherichia coli. A mutant enzyme with a different mechanism
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación SCOPUS

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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile