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Updated: Aug 22, 2026

Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
p56lyn catalyzes a reversible autophosphorylation reaction and a nucleoside diphosphate kinase reaction
C M Litwin1, M Gendreau, J H Wang
1Department of Medical Biochemistry, University of Calgary, Alberta, Canada.
Abstract:
The reversible autophosphorylation of the pp60c-src family tyrosine kinase, p56lyn has been characterized by a simple procedure that involves the examination of the enzyme catalyzed radioisotope exchange between ATP and ADP. The equilibrium constant of the reaction was determined to be 3.31 and corresponded to a standard free energy of hydrolysis of the phosphotyrosine bond in p56lyn of -8.08 kcal/mol. GDP was capable of substituting for ADP as phosphate acceptor so that p56lyn displayed a nucleoside diphosphate kinase activity.
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