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  • Title: Phosphofructokinase from Fasciola hepatica: sequence of the cAMP-dependent protein kinase phosphorylation site.
    Author: Mahrenholz AM, Hefta SA, Mansour TE.
    Journal: Arch Biochem Biophys; 1991 Aug 01; 288(2):463-7. PubMed ID: 1832841.
    Abstract:
    We have reported previously that phosphofructokinase from the liver fluke Fasciola hepatica is activated by phosphorylation with cAMP-dependent protein kinase, and that this event appears to be important in vivo for regulation of PFK (E. S. Kamemoto, L. Lan, and T. E. Mansour (1989) Arch. Biochem. Biophys. 271, 553-559). Here, we report the amino acid sequence of the single tryptic phosphopeptide generated after phosphorylation of the purified enzyme with cAMP-dependent protein kinase and [gamma 32P]ATP. Through a combination of Edman microsequence analysis, fast atom bombardment mass spectroscopy, and phosphoamino acid analysis, the sequence of the phosphorylated peptide was determined to be: R-S-T(P)-M-M-I-P-G-M-E-G-K. This sequence is not homologous to any previously determined phosphofructokinase phosphopeptides. Regulatory differences between the mammalian and parasite enzymes are discussed with particular emphasis on regulation by protein phosphorylation.
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