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Evidence for new phosphorylation sites for protein kinase C and cyclic AMP‐dependent protein kinase in bovine heart 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase
Author(s) -
Rider Mark H.,
Van Damme Josef,
Vertommen Didier,
Michel Alain,
Vandekerckhove Joël,
Hue Louis
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81315-d
Subject(s) - protein kinase a , phosphorylation , protein kinase c , biochemistry , map2k7 , mitogen activated protein kinase kinase , phosphofructokinase 2 , chemistry , kinase , protein phosphorylation , cyclin dependent kinase 2 , biology , enzyme
Bovine heart 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase (PFK‐2/FBPase‐2) was phosphorylated by incubation with [γ‐ 32 P]MgATP and cyclic AMP‐dependent protein kinase (PKA) or protein kinase C (PKC). After digestion with chymotrypsin, the phosphorylation sites for the two protein kinases were identified by peptide mapping, and microsequencing. Evidence for new phosphorylation sites for PKA (Ser‐483) and PKC (Ser‐84 and Ser‐466) was obtained.