Myofibrillar Creatine Kinase Activity Inferred from a 3D Model

Title:

Myofibrillar Creatine Kinase Activity Inferred from a 3D Model

Creator:

Jiří Mejsnar, Sopko, B., and Gergor, M.

Identifier:

https://cdk.lib.cas.cz/client/handle/uuid:d84f89ba-5145-4da7-9cfb-de662b57a26c
uuid:d84f89ba-5145-4da7-9cfb-de662b57a26c
issn:0862-8408

Subject:

Fyziologie člověka a srovnávací fyziologie, fyziologie člověka, human physiology, Muscle, Energetics, Myofibrillar creatine kinase, 14, and 612

Type:

article, studie, model:article, and TEXT

Format:

print, bez média, and svazek

Description:

Myofibrillar creatine kinase (CK) that buffers ATP during fluctuating muscle energy metabolism has been selected for studies of conformational changes underlying the cellular control of enzyme activity. The force field was computed for three energetic states, namely for the substrate-free CK molecule, for the molecule conjugated with the MgATP complex, and for the molecule conjugated with the pair of reactants MgATP-creatine. Without its substrates, the enzyme molecule assumes an inactive "open" form. Upon binding of the MgATP complex, the CK molecule takes up a reactive "closed" conformation. Subsequent binding of creatine yields a nonreactive "intermediary" conformation. Acid-base catalysis is considered to be the basic principle for the reversible transfer of the phosphoryl group between the substrates. The results indicate that the substrate-induced energy minimizing conformational changes do not represent a sufficient condition for CK activity and that some other essential component of physiological control at the cellular level is involved in the transition from the intermediary to the closed structure of the molecule., J. A. Mejsnar, B. Sopko, M. Gergor., and Obsahuje bibliografii

Language:

English

Rights:

http://creativecommons.org/licenses/by-nc-sa/4.0/
policy:public

Source:

Physiological research | 2002 Volume:51 | Number:1

Harvested from:

CDK

Metadata only:

false