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Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic
J Weekes1, K L Ball, F B Caudwell
1Department of Biochemistry, The University, Dundee, Scotland, UK.
FEBS Letters
|November 22, 1993
Abstract:
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.