Specificity determinants for the AMP‐activated protein kinase and its plant homologue analysed using synthetic peptides

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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.