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Literature summary extracted from

  • Ma, L.; Liang, S.; Jones, R.L.; Lu, Y.T.
    Characterization of a novel calcium/calmodulin-dependent protein kinase from tobacco (2004), Plant Physiol., 135, 1280-1293.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.17 Calmodulin the binding site comprises residues 913-932 with a basic amphiphilic alpha-helix structure, maximal binding at 105 nM, three different isoforms of calmodulin, CaM1, CaM3, and CaM13, differentially regulate CaMK1, overview, the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not Nicotiana tabacum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.17 construction of a cDNA library, CaMK1 DNA and amino acid sequence determination and analysis, genetic organization, expression of wild-type and mutant CaMK1s in Escherichia coli Nicotiana tabacum

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.17 L916R site-directed mutagenesis, mutation in the calmodulin binding site residue abolishes the calmodulin binding Nicotiana tabacum
2.7.11.17 R924E/K925E/K926E/K927E site-directed mutagenesis, mutations break the basic amphiphilic alpha-helix structure of the calmodulin binding site, the mutant is not capable of calmodulin binding Nicotiana tabacum
2.7.11.17 W919R site-directed mutagenesis, mutation in the calmodulin binding site residue abolishes the calmodulin binding Nicotiana tabacum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.17 additional information
-
 additional information reaction and calmodulin binding kinetics Nicotiana tabacum
2.7.11.17 0.0221
-
 syntide-2 peptide
-
 Nicotiana tabacum
2.7.11.17 0.0445
-
 histone IIIS
-
 Nicotiana tabacum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.17 Ca2+ the unphosphorylated CaMK1 is dependent on Ca2+ and calmodulin, while the autophosphorylated enzyme is not Nicotiana tabacum

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.17 Nicotiana tabacum Q84ZT8 CaMK1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.17 phosphoprotein the enzyme performs Ca2+/calmodulin-dependent autophosphorylation, which renders the enzyme independent on Ca2+ and calmodulin Nicotiana tabacum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.17 ATP + histone IIIS
-
 Nicotiana tabacum ADP + phosphorylated histone IIIS
-
 ?
2.7.11.17 ATP + syntide-2 i.e. PLARTLSVAGLPGKK, synthetic peptide substrate Nicotiana tabacum ADP + phosphorylated syntide-2
-
 ?
2.7.11.17 ATP + syntide-2 peptide syntide-2 peptide is L-prolyl-L-leucyl-L-alanyl-L-arginyl-L-threonyl-L-leucyl-L-seryl-L-valyl-L-alanylglycyl-L-leucyl-L-prolylglycyl-L-lysyl-L-lysine Nicotiana tabacum phosphorlyated syntide-2 peptide
-
 ?
2.7.11.17 additional information the enzyme performs Ca2+/calmodulin-dependent autophosphorylation Nicotiana tabacum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.17 More CaMK1 contains 11 subdomains of the kinase catalytic domain, lacks EF hands for Ca2+ binding, and is structurally similar to the mammalian enzyme Nicotiana tabacum

Synonyms

EC Number Synonyms Comment Organism
2.7.11.17 calcium/calmodulin-dependent protein kinase
-
 Nicotiana tabacum
2.7.11.17 CaM-dependent kinase
-
 Nicotiana tabacum
2.7.11.17 CaMK
-
 Nicotiana tabacum
2.7.11.17 CaMK1
-
 Nicotiana tabacum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.17 ATP
-
 Nicotiana tabacum