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

FEBS Letters

Hardie, D.Grahame²  Ball, Kathryn L.²  Caudwell, F.Barry¹  Weekes, John² 

[1] MRC Protein Phosphorylation Unit, The University, Dundee, DD1 4HN, Scotland, UK;Department of Biochemistry, The University, Dundee, DD1 4HN, Scotland, UK

关键词: AMP-activated protein kinase;    HMG-CoA reductase kinase;    Synthetic peptide;    Specificity determinant;    Consensus sequence;    Mammals;    Higher plants;    AMP-PK;    AMP-activated protein kinase;   

DOI  :  10.1016/0014-5793(93)80706-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown