Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of Creatine Kinase-Reference-Cited by-同舟云学术

Determination of the Affinity of Each Component of a Composite Quaternary Transition-State Analogue Complex of Creatine Kinase

Published:2002-05-09 Issue:22 Volume:41 Page:6995-7000
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Borders, Charles L.¹,Snider Mark J.¹,Wolfenden Richard¹,Edmiston Paul L.¹

Affiliation:

1. Department of Chemistry, The College of Wooster, Wooster, Ohio 44691, and Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi020105%2B

Reference35 articles.

1. Watts, D. C. (1973) inThe Enzymes, 3rd Ed. (Boyer, P. D., Ed.) Vol. 8, pp 383−455, Academic Press, New York.

2. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the ‘phosphocreatine circuit’ for cellular energy homeostasis

3. Evolution of Phosphagen Kinase

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