Similar substrate recognition motifs for mammalian AMP‐activated protein kinase, higher plant HMG‐CoA reductase kinase‐A, yeast SNF1, and mammalian calmodulin‐dependent protein kinase I

FEBS Letters

Hardie, D.Grahame¹  Edelman, Arthur M.²  Wilson, Wayne A.¹  Dale, Susan¹ 

[1] Department of Biochemistry, The University, Dundee, DD1 4HN, Scotland, UK;Department of Pharmacology and Toxicology, State University of New York, Buffalo, NY, USA

关键词: AMP-activated protein kinase;    HMG-CoA reductase kinase;    SNF1;    Calmodulin-dependent protein kinase I;    Specificity determinant;    Consensus sequence;    AMP-PK;    AMP-activated protein kinase;    HMG-;    3-hydroxy-3-methyl-;    HRK—A;    HMG-CoA reductase kinase-A;    SNF;    sucrose non-fermenting;    CaMKI;    calmodulin-dependent protein kinase I;    PKA;    cyclic AMP-dependent protein kinase;   

DOI  :  10.1016/0014-5793(95)00172-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have analysed phosphorylation of the synthetic peptide AMARAASAAALARRR, and 23 variants, by mammalian, higher plant and yeast members of the SNF1 protein kinase subfamily (AMP-activated protein kinase (AMPK), HMG-CoA reductase kinase (HRK-A), and SNF1 itself), and by mammalian calmodulin-dependent protein kinase I (CaMKI). These four kinases recognize motifs which are very similar, although distinguishable. Our studies define the following recognition motifs: AMPK: Φ(X,β)XXS/TXXXΦ; HRK-A: Φ(X,β)XXSXXXΦ; Snf1: ΦXRXXSXXXΦ; CaMKI: ΦXRXXS/TXXXΦ; where Φ is a hydrophobic residue (M, V, L, I or F) and β is a basic residue (R, K or H).

【 授权许可】

Unknown