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Literature summary for 2.7.11.13 extracted from
- Activation mechanisms of conventional protein kinase C isoforms are determined by the ligand affinity and conformational flexibility of their C1 domains (2003), J. Biol. Chem., 278, 46886-46894.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| diacylglycerol | binds to the C1 domains of isozymes PKCalpha and PKCgamma, differential roles of C1A and C1B, overview | Rattus norvegicus |  |
| additional information | activation mechanism of isozymes PKCalpha and PKCgamma | Rattus norvegicus | |
| phorbol 12-myristate 13-acetate | binds to the C1 domains of isozymes PKCalpha and PKCgamma, differential roles of C1A and C1B, overview | Rattus norvegicus | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of full-length isozymes PKCalpha and PKCgamma in Spodoptera frugiperda Sf9 cells using the baculovirus infection system, expression of His-tagged isolated isozymes PKCalpha and PKCgamma domains C1 in Escherichia coli strain BL21(DE3) | Rattus norvegicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D116A | site-directed mutagenesis, isozyme PKCgamma domain C1B mutant shows unaltered activity | Rattus norvegicus |
| D55A | site-directed mutagenesis, isozyme PKCalpha and PKCgamma mutants show unaltered activity and ligand binding, isozyme PKCalpha shows enhanced activation by phospholipids | Rattus norvegicus |
| W58A | site-directed mutagenesis, isozyme PKCgamma domain C1A mutant shows impaired binding of phorbol 12-myristate 13-acetate and diacylglycerol | Rattus norvegicus |
| Y123A | site-directed mutagenesis, isozyme PKCgamma domain C1B mutant shows impaired binding of phorbol 12-myristate 13-acetate and diacylglycerol | Rattus norvegicus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | binding kinetics of phorbol 12-myristate 13-acetate and diacylglycerol | Rattus norvegicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | cellular membrane translocation mechanism of isozyme PKCalpha and PKCgamma | Rattus norvegicus | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | - |
Rattus norvegicus | |
| Mg2+ | - |
Rattus norvegicus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
several isozymes | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant full-length isozymes PKCalpha and PKCgamma from Sf9 cells by ion exchange chromatography, recombinant His-tagged isolated isozymes PKCalpha and PKCgamma domains C1 from Escherichia coli strain BL21(DE3) inclusion bodies by nickel affinity chromatography | Rattus norvegicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + histone III-SS | commercial substrate | Rattus norvegicus | ADP + phosphorylated histone III-SS | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PKC | - |
Rattus norvegicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Rattus norvegicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Rattus norvegicus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Rattus norvegicus | |
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Release 2023.1 (January 2023)
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