Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 3. Mechanism
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
Grantová podpora
R01 GM077551
NIGMS NIH HHS - United States
GM 77551
NIGMS NIH HHS - United States
PubMed
19719322
PubMed Central
PMC2758332
DOI
10.1021/bi900281s
Knihovny.cz E-zdroje
- MeSH
- adenosindifosfát chemie metabolismus MeSH
- aktivace enzymů MeSH
- alosterická regulace MeSH
- chemické modely MeSH
- energetický metabolismus MeSH
- fenylalanin chemie MeSH
- kosterní svaly enzymologie MeSH
- králíci MeSH
- ligandy MeSH
- počítačová simulace MeSH
- pyruvátkinasa antagonisté a inhibitory chemie metabolismus fyziologie MeSH
- termodynamika MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
- Názvy látek
- adenosindifosfát MeSH
- fenylalanin MeSH
- ligandy MeSH
- pyruvátkinasa MeSH
Mammalian pyruvate kinase exists in four isoforms with characteristics tuned to specific metabolic requirements of different tissues. All of the isoforms, except the muscle isoform, exhibit typical allosteric behavior. The case of the muscle isoform is a conundrum. It is inhibited by an allosteric inhibitor, Phe, yet it has traditionally not been considered as an allosteric enzyme. In this series of study, an energetic landscape of rabbit muscle pyruvate kinase (RMPK) was established. The phenomenon of inhibition by Phe is shown to be physiological. Furthermore, the thermodynamics for the temperature fluctuation and concomitant pH change as a consequence of muscle activity were elucidated. 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 <--> 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.
Zobrazit více v PubMed
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In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies