Phosphorylation of lactate dehydrogenase by ATP.
Evidence is presented indicating that phosphorylation of porcine muscle lactate dehydrogenase by [gamma-32P] ATP occurs at carboxyl residues of the protein. The phosphoenzyme complex was moderately stable at pH 6.8 and 25 degrees C, with a half-life of 3.5 h. In the presence of NADH rapid dephosphorylation occurred. Formation of an abortive complex with NAD-pyruvate also caused hydrolysis of the phosphoenzyme. The phosphorylated lactate dehydrogenase was shown to serve as a phosphate donor for phosphorylation of ADP.
Yasykova MYu
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Vener
A V
AV
Muronetz
V I
VI
Nagradova
N K
NK
D000255:Adenosine Triphosphate / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002855:Chromatography, Thin Layer; D004795:Enzyme Stability; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D010766:Phosphorylation; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid
D011773:Pyruvates; D009243:NAD; D019289:Pyruvic Acid; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase