About: Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 3. Mechanism     Goto   Sponge   NotDistinct   Permalink

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  • We have shown that (1) the differential number of protons released or absorbed with regard to the various linked reactions adds another level of control to shift the binding constants and equilibrium of active reversible arrow inactive state changes (the latter controls quantitatively the activity of RMPK); (2) ADP plays a major role in the allosteric mechanism in RMPK under physiological temperatures (depending on the temperature, ADP can assume dual and opposite roles of being an inhibitor by binding preferentially to the inactive form and a substrate); and (3) simulation of the RMPK behavior under physiological conditions shows that the net results of the 21 thermodynamic parameters involved in the regulation are well-tuned to allow the maximal response of the enzyme to even minute changes in temperature and ligand concentration.
  • We have shown that (1) the differential number of protons released or absorbed with regard to the various linked reactions adds another level of control to shift the binding constants and equilibrium of active reversible arrow inactive state changes (the latter controls quantitatively the activity of RMPK); (2) ADP plays a major role in the allosteric mechanism in RMPK under physiological temperatures (depending on the temperature, ADP can assume dual and opposite roles of being an inhibitor by binding preferentially to the inactive form and a substrate); and (3) simulation of the RMPK behavior under physiological conditions shows that the net results of the 21 thermodynamic parameters involved in the regulation are well-tuned to allow the maximal response of the enzyme to even minute changes in temperature and ligand concentration. (en)
Title
  • Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 3. Mechanism
  • Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 3. Mechanism (en)
skos:prefLabel
  • Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 3. Mechanism
  • Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 3. Mechanism (en)
skos:notation
  • RIV/00216208:11320/09:00206689!RIV10-MSM-11320___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM0021620835)
http://linked.open...iv/cisloPeriodika
  • 40
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 315710
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11320/09:00206689
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Functional; Energetic; Landscape; Allosteric; Regulation; Muscle; Pyruvate; Kinase; Mechanism (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [EEC2B462A0C0]
http://linked.open...i/riv/nazevZdroje
  • Biochemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 48
http://linked.open...iv/tvurceVysledku
  • Heřman, Petr
  • Lee, James C.
http://linked.open...ain/vavai/riv/wos
  • 000270459100017
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-2960
number of pages
http://localhost/t...ganizacniJednotka
  • 11320
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