Distinguishing between closely related protein kinases: A variation on the bisubstrate inhibitor theme

Journal of the American Chemical Society

Volumn 118, Issue 26, 1996, Pages 6321-6322

  Yan, Xiongwei ^a   Lawrence, David S ^a   Corbin, Jackie D ^b   Francis, Sharron H ^b  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE;

ARTICLE; ENZYME ASSAY; ENZYME INHIBITION; ENZYME SPECIFICITY; TECHNIQUE;

EID: 0030061201     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9609213     Document Type: Article

References (35)

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19. 5 in the PKA-catalyzed reaction. Unfortunately, the latter arginine-rich peptide substrate cannot be employed with PKG since, in addition to serving as a substrate for this enzyme, it also appears to bind to a "polyarginine binding site" (Walton, G. M.; Gill, G. N. J. Biol. Chem. 1981, 256, 1681-1688), which significantly modulates PKG activity (Yan, X.; Lawrence, D. S. Unpublished results).
20. 5 in the PKA-catalyzed reaction. Unfortunately, the latter arginine-rich peptide substrate cannot be employed with PKG since, in addition to serving as a substrate for this enzyme, it also appears to bind to a "polyarginine binding site" (Walton, G. M.; Gill, G. N. J. Biol. Chem. 1981, 256, 1681-1688), which significantly modulates PKG activity (Yan, X.; Lawrence, D. S. Unpublished results).
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