The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates

Ou, Yang; Tao, Wenbing; Zhang, Yun; Wu, Guangrong; Yu, Shaoning

doi:10.1016/j.ijbiomac.2010.04.017

Cited by 5 publications

(6 citation statements)

References 20 publications

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“…, increase the solvent exposure of Trp-157. Compared to the previous study, these results clearly indicate that the majority of changes in tryptophan fluorescence signal from PK induced by the binding of activating cations come from Trp-157 (Kayne and Suelter 1965;Ou et al 2010;Suelter 1967).…”

Section: Interaction With Activating Cationscontrasting

confidence: 50%

“…and K ? lead to more exposed tryptophan residues of PK while interactions with PEP and ADP decreased solvent accessibility of the tryptophan residues (Ou et al 2010). However, the results cannot confirm the contribution of every tryptophan residue on the fluorescence signal changes of PK induced by ligand binding.…”

Section: Introductionmentioning

confidence: 80%

“…A variety of techniques have been used to explore changes in the conformation of pyruvate kinase in response to ligand binding (Carminat et al 1971; Kayne and Price 1972;Kayne and Suelter 1965;Cohn 1965, 1966;Oria-Hernandez et al 2005;Ou et al 2010;Suelter 1967;Suelter et al 1966;Yu et al 2003). Kinetic data Feng Li and Ting Yu equally contribute to this work.…”

Section: Introductionmentioning

confidence: 99%

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Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching

Zhao

et al. 2012

Eur Biophys J

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Pyruvate kinase acts as an allosteric enzyme, playing a crucial role in the catalysis of the final step of the glycolytic pathway. In this study, site-specific mutagenesis and tryptophan fluorescence quenching were used to probe the catalytic allosteric mechanism of rabbit muscle pyruvate kinase. Movement of the B domain was found to be essential for the catalytic reaction. Rotation of the B domain in the opening of the cleft between domains B and A induced by the binding of activating cations allows substrates to bind, whereas substrate binding shifts the rotation of the B domain in the closure of the cleft. Trp-157 accounts for the differences in tryptophan fluorescence signal with and without activating cations and substrates. Trp-481 and Trp-514 are brought into an aqueous environment after phenylalanine binding.

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Section: Interaction With Activating Cationscontrasting

confidence: 50%

Section: Introductionmentioning

confidence: 80%

Section: Introductionmentioning

confidence: 99%

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Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching

Zhao

et al. 2012

Eur Biophys J

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“…In addition to a monovalent cation, most PyKs require a divalent (Mg 2+ or Mn 2+ ) cation, which has been implicated in enzyme activation and in the formation of the substrate‐complex with ADP . Cations have also been suggested to induce domain movement . Amino acids responsible for binding to the divalent cation are within the A‐domain .…”

Section: Architecture Of Pyksmentioning

confidence: 99%

“…61 Cations have also been suggested to induce domain movement. 62 Amino acids responsible for binding to the divalent cation are within the A-domain. [63][64][65] In LmPyK 10 the Mg 2+ ion (or Mn 2+ ) interacts with the carboxylate side chains of Glu241 and Asp265.…”

Section: Active Sitementioning

confidence: 99%

An overview of structure, function, and regulation of pyruvate kinases

et al. 2019

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In the last step of glycolysis Pyruvate kinase catalyzes the irreversible conversion of ADP and phosphoenolpyruvate to ATP and pyruvic acid, both crucial for cellular metabolism. Thus pyruvate kinase plays a key role in controlling the metabolic flux and ATP production. The hallmark of the activity of different pyruvate kinases is their tight modulation by a variety of mechanisms including the use of a large number of physiological allosteric effectors in addition to their homotropic regulation by phosphoenolpyruvate. Binding of effectors signals precise and orchestrated movements in selected areas of the protein structure that alter the catalytic action of these evolutionarily conserved enzymes with remarkably conserved architecture and sequences. While the diverse nature of the allosteric effectors has been discussed in the literature, the structural basis of their regulatory effects is still not well understood because of the lack of data representing conformations in various activation states. Results of recent studies on pyruvate kinases of different families suggest that members of evolutionarily related families follow somewhat conserved allosteric strategies but evolutionarily distant members adopt different strategies. Here we review the structure and allosteric properties of pyruvate kinases of different families for which structural data are available.

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Effects of activating cations and inhibitor on the allosteric regulation of rabbit muscle pyruvate kinase

Jiang

et al. 2013

International Journal of Biological Macromolecules

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The conformational change of rabbit muscle pyruvate kinase induced by activating cations and its substrates

Cited by 5 publications

References 20 publications

Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching

Probing the catalytic allosteric mechanism of rabbit muscle pyruvate kinase by tryptophan fluorescence quenching

An overview of structure, function, and regulation of pyruvate kinases

Effects of activating cations and inhibitor on the allosteric regulation of rabbit muscle pyruvate kinase

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