Abstract
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: phi (X beta)XXS/TXXX phi; HRK-A: phi (X,beta)XXSXXX phi; Snf1: phi XRXXSXXX phi; CaMKI: phi XRXXS/TXXX phi; where phi is a hydrophobic residue (M, V, L, I or F) and beta is a basic residue (R, K or H).
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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AMP-Activated Protein Kinases
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Amino Acid Sequence
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Animals
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Binding Sites
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Mammals
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Molecular Sequence Data
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Multienzyme Complexes / metabolism*
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Oligopeptides / chemical synthesis
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Oligopeptides / chemistry
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Oligopeptides / metabolism
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Phosphorylation
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Plants / enzymology
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Protein Kinases / metabolism*
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Protein-Serine-Threonine Kinases / metabolism*
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Saccharomyces cerevisiae / metabolism
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Multienzyme Complexes
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Oligopeptides
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Protein Kinases
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SNF1-related protein kinases
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Protein-Serine-Threonine Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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AMP-Activated Protein Kinases