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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
[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).

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[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 [时效性] 
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