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SPECIFICITY DETERMINANTS FOR THE AMP-ACTIVATED PROTEIN-KINASE AND ITS PLANT HOMOLOG ANALYZED USING SYNTHETIC PEPTIDES
被引:83
|作者:
WEEKES, J
BALL, KL
CAUDWELL, FB
HARDIE, DG
机构:
[1] UNIV DUNDEE,DEPT BIOCHEM,DUNDEE DD1 4HN,SCOTLAND
[2] UNIV DUNDEE,MRC,PROTEIN PHOSPHORYLAT UNIT,DUNDEE DD1 4HN,SCOTLAND
基金:
英国惠康基金;
关键词:
AMP-ACTIVATED PROTEIN KINASE;
HMG-COA REDUCTASE KINASE;
SYNTHETIC PEPTIDE;
SPECIFICITY DETERMINANT;
CONSENSUS SEQUENCE;
MAMMALS;
HIGHER PLANTS;
D O I:
10.1016/0014-5793(93)80706-Z
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
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.
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页码:335 / 339
页数:5
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