FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1489262601> ?p ?o ?g. }

• W1489262601 endingPage "680" @default.
• W1489262601 startingPage "674" @default.
• W1489262601 abstract "Abstract The catalytic activity of yeast phosphofructokinase is dependent on the concentrations of both uncomplexed Mg2+ and MgITP2-, and not on the concentration of uncomplexed ITP. The allosteric inhibition of catalysis by ATP is dependent on the concentration of MgATP2- and not on the concentration of uncomplexed ATP. It is proposed that the nucleoside triphosphate substrates are bound as Mg2+ complexes, that catalysis requires uncomplexed Mg2+, and that MgATP2- is the negative effector. Addition of NH4Cl increases the catalytic activity of yeast phosphofructokinase up to 20-fold depending on the allosteric state of the enzyme. This activation can be resolved into the formation of two NH4+-enzyme complexes. Formation of the stronger complex, which has an apparent dissociation constant of 3 mm, produces about a 100% increase in the rate of catalysis irrespective of the allosteric state of the enzyme. Formation of the weaker complex is only detected catalytically in the presence of low concentrations of the positive effector, fructose-6-P, or in the presence of the negative effector, MgATP2-. The apparent dissociation constant of the weaker NH4+-enzyme complex increases as the concentration of the positive effector decreases or the concentration of negative effector increases, or both. The presence of 50 mm NH4Cl increases the affinity of the enzyme for the substrate fructose-6-P and decreases the Hill coefficient of fructose-6-P. It was concluded that NH4+ functions as an activator when binding to the stronger site and as a positive allosteric effector when binding to the weaker site. Addition of KCl also increases the catalytic activity of the enzyme. This activation can be resolved into the formation of two K+-enzyme complexes. Formation of the stronger complex, which has an apparent dissociation constant of about 10 mm, produces a 50% increase in catalytic activity and does not appear to alter the allosteric state of the enzyme. Although the apparent dissociation constant of the weaker K+-enzyme complex increases as the initial concentration of positive effector decreases or negative effector increases (or both), the presence of 200 mm KCl does not change the affinity of the enzyme for fructose-6-P or the Hill coefficient of this substrate. It was concluded therefore that K+ is not a significant allosteric effector. Competition experiments indicate that the stronger NH4+ and K+ sites are distinct from each other and that the catalytic response to the binding of NH4+ and K+ to these sites is not additive." @default.
• W1489262601 created "2016-06-24" @default.
• W1489262601 creator A5034742753 @default.
• W1489262601 creator A5077187127 @default.
• W1489262601 date "1970-02-01" @default.
• W1489262601 modified "2023-09-26" @default.
• W1489262601 title "The Role of Cations in Yeast Phosphofructokinase Catalysis" @default.
• W1489262601 cites W121598433 @default.
• W1489262601 cites W1435468342 @default.
• W1489262601 cites W1519104132 @default.
• W1489262601 cites W1540662041 @default.
• W1489262601 cites W1572582386 @default.
• W1489262601 cites W1601568825 @default.
• W1489262601 cites W1603868171 @default.
• W1489262601 cites W1627487191 @default.
• W1489262601 cites W1968085060 @default.
• W1489262601 cites W1968243869 @default.
• W1489262601 cites W1994203632 @default.
• W1489262601 cites W1998093640 @default.
• W1489262601 cites W2005392755 @default.
• W1489262601 cites W2016624705 @default.
• W1489262601 cites W2046413874 @default.
• W1489262601 cites W2054382041 @default.
• W1489262601 cites W2068983843 @default.
• W1489262601 cites W2074581799 @default.
• W1489262601 cites W2091508479 @default.
• W1489262601 cites W2135512849 @default.
• W1489262601 cites W2139951598 @default.
• W1489262601 cites W95753805 @default.
• W1489262601 doi "https://doi.org/10.1016/s0021-9258(18)63315-0" @default.
• W1489262601 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4244536" @default.
• W1489262601 hasPublicationYear "1970" @default.
• W1489262601 type Work @default.
• W1489262601 sameAs 1489262601 @default.
• W1489262601 citedByCount "56" @default.
• W1489262601 countsByYear W14892626012015 @default.
• W1489262601 countsByYear W14892626012016 @default.
• W1489262601 countsByYear W14892626012022 @default.
• W1489262601 crossrefType "journal-article" @default.
• W1489262601 hasAuthorship W1489262601A5034742753 @default.
• W1489262601 hasAuthorship W1489262601A5077187127 @default.
• W1489262601 hasBestOaLocation W14892626011 @default.
• W1489262601 hasConcept C122245378 @default.
• W1489262601 hasConcept C161790260 @default.
• W1489262601 hasConcept C185592680 @default.
• W1489262601 hasConcept C20251656 @default.
• W1489262601 hasConcept C2779222958 @default.
• W1489262601 hasConcept C55493867 @default.
• W1489262601 hasConcept C62231903 @default.
• W1489262601 hasConceptScore W1489262601C122245378 @default.
• W1489262601 hasConceptScore W1489262601C161790260 @default.
• W1489262601 hasConceptScore W1489262601C185592680 @default.
• W1489262601 hasConceptScore W1489262601C20251656 @default.
• W1489262601 hasConceptScore W1489262601C2779222958 @default.
• W1489262601 hasConceptScore W1489262601C55493867 @default.
• W1489262601 hasConceptScore W1489262601C62231903 @default.
• W1489262601 hasIssue "4" @default.
• W1489262601 hasLocation W14892626011 @default.
• W1489262601 hasOpenAccess W1489262601 @default.
• W1489262601 hasPrimaryLocation W14892626011 @default.
• W1489262601 hasRelatedWork W2000372697 @default.
• W1489262601 hasRelatedWork W2010669773 @default.
• W1489262601 hasRelatedWork W2066589921 @default.
• W1489262601 hasRelatedWork W2070828966 @default.
• W1489262601 hasRelatedWork W2167690733 @default.
• W1489262601 hasRelatedWork W2413381278 @default.
• W1489262601 hasRelatedWork W2417976177 @default.
• W1489262601 hasRelatedWork W2423912402 @default.
• W1489262601 hasRelatedWork W2424216230 @default.
• W1489262601 hasRelatedWork W4211064073 @default.
• W1489262601 hasVolume "245" @default.
• W1489262601 isParatext "false" @default.
• W1489262601 isRetracted "false" @default.
• W1489262601 magId "1489262601" @default.
• W1489262601 workType "article" @default.