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

FEBS Lett. 1993 Nov 22;334(3):335-9. doi: 10.1016/0014-5793(93)80706-z.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Acetyl-CoA Carboxylase / metabolism
  • Amino Acid Sequence
  • Animals
  • Glycogen Synthase / metabolism
  • Humans
  • Liver / enzymology
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Peptides / chemical synthesis
  • Plants / enzymology*
  • Protein Kinases / metabolism*
  • Protein-Serine-Threonine Kinases*
  • Rats
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Multienzyme Complexes
  • Peptides
  • Glycogen Synthase
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Acetyl-CoA Carboxylase