Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 2. Fluorescence Study

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F09%3A00207044" target="_blank" >RIV/00216208:11320/09:00207044 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Functional Energetic Landscape in the Allosteric Regulation of Muscle Pyruvate Kinase. 2. Fluorescence Study

Original language description

Four novel insights were uncovered. (1) ADP exhibits a dual property. Depending on the temperature, ADP can regulate RMPK activity by switching the enzyme to either the R or T state. (2) The assumption that ligand binding to RMPK is state-dependent is only correct for PEP but not Phe and ADP. (3) The effect of pH on the regulatory behavior of RMPK is partly due to the complex pattern of proton release or absorption linked to the multiple linked equilibria which govern the activity of the enzyme. (4) TheR {-} T equilibrium is accompanied by a significant Delta C-p, rendering RMPK most sensitive to temperature under physiological conditions.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

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Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2009

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Biochemistry

ISSN

0006-2960

e-ISSN

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Volume of the periodical

40

Issue of the periodical within the volume

40

Country of publishing house

US - UNITED STATES

Number of pages

10

Pages from-to

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UT code for WoS article

000270459100016

EID of the result in the Scopus database

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