Unraveling The Catalytic Mechanism Of Phosphofructokinase-2 From E. Coli: A Qm/Mm Theoretical Study

dc.date.accessioned2019-03-27T15:58:55Z
dc.date.accessioned2022-10-18T22:15:05Z
dc.date.available2019-03-27T15:58:55Z
dc.date.available2022-10-18T22:15:05Z
dc.date.created2019-03-27T15:58:55Z
dc.date.issued2016
dc.identifierhttp://hdl.handle.net/10533/234639
dc.identifier1140618
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4465996
dc.description.abstractThe ATP-dependent phosphorylation of fructose-6-phosphate, named phosphofructokinase (PFK) activity, is one of the most important steps in the glycolytic pathway; this is why it is highly regulated in a wide variety of organisms. Escherichia coli has two
dc.languageeng
dc.relation39°
dc.relationinfo:eu-repo/grantAgreement/Fondecyt/1140618
dc.relationReunión Anual de la Sociedad de Bioquímica y Biología Molecular de Chile
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleUnraveling The Catalytic Mechanism Of Phosphofructokinase-2 From E. Coli: A Qm/Mm Theoretical Study
dc.typePonencia


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