Specificity determinants for the AMP-activated protein kinase and its plant homologue analysed using synthetic peptides.
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.
Weekes
J
J
Department of Biochemistry, The University, Dundee, Scotland, UK.
Ball
K L
KL
Caudwell
F B
FB
Hardie
D G
DG
D055372:AMP-Activated Protein Kinases; D000103:Acetyl-CoA Carboxylase / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D006006:Glycogen Synthase / Q000378:metabolism; D006801:Humans; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000378:metabolism*; D010455:Peptides / Q000138:chemical synthesis; D010944:Plants / Q000201:enzymology*; D011494:Protein Kinases / Q000378:metabolism*; D017346:Protein Serine-Threonine Kinases; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D009097:Multienzyme Complexes; D010455:Peptides; D006006:Glycogen Synthase; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases; D000103:Acetyl-CoA Carboxylase