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Specificity determinants for the AMP‐activated protein kinase and its plant homologue analysed using synthetic peptides
Author(s) -
Weekes John,
Ball Kathryn L.,
Caudwell F.Barry,
Hardie D.Grahame
Publication year - 1993
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(93)80706-z
Subject(s) - kinase , protein kinase a , residue (chemistry) , biochemistry , chemistry , stereochemistry , biology
Inspection of sequences around sites phosphorylated by the AMP‐activated protein kinase (AMP‐PK), and homologous sequences from other species, indicates conserved features. There are hydrophobic residues (M, V, L, I) at P‐5 and P+4, and at least one basic residue (R, K, H) at P‐2, P‐3 or P‐4. The importance of these residues has been established for AMP‐PK and its putative plant homologue using a series of synthetic peptides. These results confirm the functional similarity of the animal and plant kinases, and suggest that the required motif for recognition of substrate by either kinase is M/V/L/I‐(R/K/H,X,X)‐X‐S/T‐X‐X‐X‐M/V/L/I.