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Identity and substrate specificity of human erythrocyte membrane‐bound and cytosolic casein kinases
Author(s) -
T Wei,
M Tao
Publication year - 1991
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(91)80852-t
Subject(s) - casein kinase 1 , biochemistry , kinase , casein kinase 2 , phosphorylation , casein kinase 2, alpha 1 , enzyme , protease , chemistry , biology , protein kinase c , protein kinase a , mitogen activated protein kinase kinase
The relationship and substrate specificity of the human erythrocyte membrane kinase and casein kinase A were investigated. Based on Staphylococcus aureus V8 protease digestion patterns, the 2 kinases appeared to be structurally homologous. These enzymes also exhibited the same substrate specificity and phosphorylated the same synthetic peptides and domains of ankyrin. Both kinases did not utilize GTP effectively as a substrate and were not inhibited by low concentrations of heparin, suggesting that they were type 1 casein kinases. An analysis of synthetic peptide phosphorylation failed to reveal a specific pattern of recognition of the amino acid sequence surrounding the phosphorylation site.