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Phosphorylation of the sarcoplasmic calcium-activated adenosinetriphosphatase as studied by /sup 31/P nuclear magnetic resonance

Journal Article · · Biochemistry; (United States)
OSTI ID:5720931
A reinvestigation of a study in which the /sup 31/P nuclear magnetic resonance (NMR) signal of the phosphointermediate of the sarcoplasmic (Ca/sup 2 +/, Mg/sup 2 +/)-ATPase has been identified shows that the signal described most probably originates from free Mg x ATP but not from the phosphoenzyme itself. It was possible to detect the /sup 31/P NMR signal of the phosphoenzyme in peptic fragments of sarcoplasmic ATPase phosphorylated either by ATP or by inorganic phosphate. The two products exhibit the same spectral characteristics in /sup 31/P NMR, implying that most probably both reaction pathways yield the same chemical product. Chemical shifts at low pH (-6.5 ppm) and high pH (-1.4 ppm) of the phosphoryl group are indicative of a ..beta..-phosphoaspartyl moiety, thus confirming independently the results from chemical analysis. The relatively low pK value of 4.3 of the phosphoryl group suggests an interaction with a positively charged group of the enzyme.
Research Organization:
Max Planck Institute for Medical Research, Heidelberg, West Germany
OSTI ID:
5720931
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:10; ISSN BICHA
Country of Publication:
United States
Language:
English