Open AccessTransient‐Phase Studies on the Arginine Kinase Reaction
Author(s) -
BARMAN Thomas E.,
TRAVERS Franck,
BERTRAND Raoul,
ROSEAU Gilbert
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb20919.x
Subject(s) - arginine kinase , arginine , chemistry , enzyme , kinetics , creatine kinase , phosphate , biochemistry , biophysics , amino acid , biology , physics , quantum mechanics
1 The initial formation of arginine phosphate by arginine kinase was studied in the time range 2.8–50 ms by the quenched‐flow method. 2 A transient burst phase of product formation was obtained, the amplitude of which was temperature‐dependent. At 35 °C it was 0.64 mol arginine phosphate/mol arginine kinase and at 12 °C, 0.25 mol/mol. 3 These results show that for the reaction pathway of arginine kinase the rate‐limiting step follows the formation of arginine phosphate on the enzyme. This is in contrast to the creatine kinase reaction where no transient phase was observed [Engelborghs, Y., Marsh, A. & Gutfreund, H. (1975) Biochem. J. 151 , 47–50]. 4 The rate‐limiting step on the arginine kinase reaction pathway is only slightly affected by temperature: the change in k cat with temperature is due to a change of an equilibrium constant pertaining to at least two previous steps.