FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1481006558> ?p ?o ?g. }

• W1481006558 endingPage "12941" @default.
• W1481006558 startingPage "12935" @default.
• W1481006558 abstract "We re-examined the kinetics of the bisphosphatase reaction of rat hepatic 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase after depleting the enzyme of bound fructose 6-phosphate and found a hyperbolic dependence on fructose 2,6-bisphosphate at concentrations below 100 nM. The Michaelis constant was 4 nM, the Vmax was about 12 nmol X mg-1 X min-1 at 22 degrees C but the substrate inhibited at concentrations above 100 nM. Both phosphate and alpha-glycerol phosphate strongly inhibited phosphoenzyme formation and hydrolytic rate below 100 nM, but relieved the inhibition by substrate at higher concentrations probably by antagonizing substrate binding. A number of observations support the proposition that the phosphoenzyme is a necessary participant in catalysis. 1) The amount of phosphoenzyme measured during steady-state hydrolysis as a function of substrate concentration correlated with the velocity profile. 2) Rapid mixing experiments demonstrated that over a broad range of substrate concentrations phosphoenzyme formation was faster than the net rate of hydrolysis. 3) Both phosphate and alpha-glycerol phosphate inhibited the rate of phosphoenzyme formation and, at low substrate concentrations, reduced the steady-state phosphoenzyme levels. The latter correlated with inhibition of substrate hydrolysis. 4) Both phosphate and alpha-glycerol phosphate stimulate the rate of phosphoenzyme breakdown, consistent with their stimulation of substrate hydrolysis at high substrate concentrations. 5) The fractional rate of phosphoenzyme breakdown, which was pH and substrate dependent, multiplied by the amount of phosphoenzyme obtained in the steady state at that pH and substrate concentration approximated the observed rate of hydrolysis. We conclude that the phosphoenzyme is a reaction intermediate in the hepatic fructose-2,6-bisphosphatase reaction." @default.
• W1481006558 created "2016-06-24" @default.
• W1481006558 creator A5002228234 @default.
• W1481006558 creator A5048018962 @default.
• W1481006558 creator A5078482941 @default.
• W1481006558 date "1985-10-01" @default.
• W1481006558 modified "2023-09-29" @default.
• W1481006558 title "Evidence for a phosphoenzyme intermediate in the reaction pathway of rat hepatic fructose-2,6-bisphosphatase." @default.
• W1481006558 cites W1490843190 @default.
• W1481006558 cites W1508384599 @default.
• W1481006558 cites W1516648662 @default.
• W1481006558 cites W1516876967 @default.
• W1481006558 cites W1530556352 @default.
• W1481006558 cites W1534163737 @default.
• W1481006558 cites W1545663938 @default.
• W1481006558 cites W1547277102 @default.
• W1481006558 cites W1567530835 @default.
• W1481006558 cites W1568680367 @default.
• W1481006558 cites W1571686660 @default.
• W1481006558 cites W1591608688 @default.
• W1481006558 cites W1595095757 @default.
• W1481006558 cites W1638928527 @default.
• W1481006558 cites W1993364219 @default.
• W1481006558 cites W1998388006 @default.
• W1481006558 cites W2004231513 @default.
• W1481006558 cites W2004529487 @default.
• W1481006558 cites W2017373178 @default.
• W1481006558 cites W2026232852 @default.
• W1481006558 cites W2031533459 @default.
• W1481006558 cites W2074432086 @default.
• W1481006558 cites W2121631413 @default.
• W1481006558 cites W2172107587 @default.
• W1481006558 cites W26309257 @default.
• W1481006558 cites W51014345 @default.
• W1481006558 cites W92174569 @default.
• W1481006558 doi "https://doi.org/10.1016/s0021-9258(17)38815-4" @default.
• W1481006558 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2997149" @default.
• W1481006558 hasPublicationYear "1985" @default.
• W1481006558 type Work @default.
• W1481006558 sameAs 1481006558 @default.
• W1481006558 citedByCount "50" @default.
• W1481006558 crossrefType "journal-article" @default.
• W1481006558 hasAuthorship W1481006558A5002228234 @default.
• W1481006558 hasAuthorship W1481006558A5048018962 @default.
• W1481006558 hasAuthorship W1481006558A5078482941 @default.
• W1481006558 hasBestOaLocation W14810065581 @default.
• W1481006558 hasConcept C185592680 @default.
• W1481006558 hasConcept C189909181 @default.
• W1481006558 hasConcept C2776970464 @default.
• W1481006558 hasConcept C55493867 @default.
• W1481006558 hasConcept C71240020 @default.
• W1481006558 hasConcept C86803240 @default.
• W1481006558 hasConcept C95444343 @default.
• W1481006558 hasConceptScore W1481006558C185592680 @default.
• W1481006558 hasConceptScore W1481006558C189909181 @default.
• W1481006558 hasConceptScore W1481006558C2776970464 @default.
• W1481006558 hasConceptScore W1481006558C55493867 @default.
• W1481006558 hasConceptScore W1481006558C71240020 @default.
• W1481006558 hasConceptScore W1481006558C86803240 @default.
• W1481006558 hasConceptScore W1481006558C95444343 @default.
• W1481006558 hasIssue "24" @default.
• W1481006558 hasLocation W14810065581 @default.
• W1481006558 hasOpenAccess W1481006558 @default.
• W1481006558 hasPrimaryLocation W14810065581 @default.
• W1481006558 hasRelatedWork W1601079487 @default.
• W1481006558 hasRelatedWork W1966862125 @default.
• W1481006558 hasRelatedWork W2004231513 @default.
• W1481006558 hasRelatedWork W2008102720 @default.
• W1481006558 hasRelatedWork W2045534958 @default.
• W1481006558 hasRelatedWork W2048642571 @default.
• W1481006558 hasRelatedWork W2053826987 @default.
• W1481006558 hasRelatedWork W2069966822 @default.
• W1481006558 hasRelatedWork W2074675460 @default.
• W1481006558 hasRelatedWork W2149568310 @default.
• W1481006558 hasVolume "260" @default.
• W1481006558 isParatext "false" @default.
• W1481006558 isRetracted "false" @default.
• W1481006558 magId "1481006558" @default.
• W1481006558 workType "article" @default.