Phosphorylation of lactate dehydrogenase by ATP
Yasykova MYu; Vener, A.V.; Muronetz, V.I.; Nagradova, N.K.
Biochemistry International 17(1): 133-139
1988
ISSN/ISBN: 0158-5231 PMID: 3190711 Document Number: 324140
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.