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
来源：
FEBS LETTERS | 1993年 / 334卷 / 03期
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.
引用
收藏
页码：335 / 339
页数：5
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