Changing the substrate specificity of creatine kinase from creatine to glycocyamine: Evidence for a highly evolved active site-Reference-Cited by-同舟云学术

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Changing the substrate specificity of creatine kinase from creatine to glycocyamine: Evidence for a highly evolved active site

Published:2007-12 Issue:12 Volume:1774 Page:1519-1527
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Jourden Michael J.,Clarke Callisia N.,Palmer Allyson K.,Barth Emily J.,Prada Rebecca C.,Hale Robyn N.,Fraga Dean,Snider Mark J.,Edmiston Paul L.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference52 articles.

1. Evolution and physiological roles of phosphagen systems;Ellington;Annu. Rev. Physiol.,2001

2. Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase);Watts,1973

3. The creatine-creatine phosphate energy shuttle;Bessman;Ann. Rev. Biochem.,1985

4. Arginine kinase evolved twice: evidence that echinoderm arginine kinase originated from creatine kinase;Suzuki;Biochem. J.,1999

5. E.O. Anosike, B.H. Moreland, D.C. Watts, Evolutionary variation between a monomer and a dimer arginine kinase, Biochem. J. 145 (175) 535–543.

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3. Submembranous recruitment of creatine kinase B supports formation of dynamic actin-based protrusions of macrophages and relies on its C-terminal flexible loop;European Journal of Cell Biology;2015-02

4. Gene structure of the two-domain taurocyamine kinase from Paragonimus westermani : Evidence for a distinct lineage of trematode phosphagen kinases;FEBS Letters;2013-06-07

5. Protein Conformational Disorder and Enzyme Catalysis;Dynamics in Enzyme Catalysis;2013

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