Phosphorylation of D-glyceraldehyde-3-phosphate dehydrogenase by Ca2+/calmodulin-dependent protein kinase II.
Rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase was shown to serve as a substrate for Ca2+/calmodulin-dependent protein kinase II with a Km of 0.33 microM and a Vmax of 2.63 mumol.min-1.mg-1 at pH 7.5 and 30 degrees C. In the absence of calmodulin, the Vmax was halved and Km unchanged. 0.99 mol of phosphate was incorporated per tetrameric molecule of D-glyceraldehyde-3-phosphate dehydrogenase under the experimental conditions employed.
Ashmarina
L I
LI
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Louzenko
S E
SE
Severin
S E
SE
Muronetz
V I
VI
Nagradova
N K
NK
D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases; D002147:Calmodulin / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D009124:Muscle Proteins / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011817:Rabbits
D002147:Calmodulin; D009124:Muscle Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011494:Protein Kinases; D017871:Calcium-Calmodulin-Dependent Protein Kinases