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Literature summary for 2.7.11.24 extracted from
- Kinetic mechanism for p38 MAP kinase alpha. A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate (2005), FEBS J., 272, 4631-4645.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the recombinant detagged enzyme is activated by specific phosphorylation at Thr180 and Tyr182 through recombinant GST-tagged MKK6 mutant S207E/T211E | Mus musculus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of GST-tagged p38 isozyme alpha in Escherichia coli strain BL21(DE3) | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| adenylyl-beta,gamma-methylene diphosphonic acid | i.e. AMP-PCP, MgAMP-PCP shows a mixed inhibition pattern in the kinase reaction, and a competitive pattern in the ATPase reaction | Mus musculus |  |
| ADP | MgADP- shows an uncompetitive inhibition pattern | Mus musculus | |
| AMP-PCP | - |
Mus musculus | |
| additional information | no inhibition by AMP and adenine | Mus musculus | |
| SB203580 | noncompetitive in the kinase reaction, competitive versus ATP in the ATPase reaction, no classical linear inhibition kinetics at concentrations below 100 nM | Mus musculus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetics, kinetic mechanism for p38 MAP kinase alpha kinase and ATPase activities, overview | Mus musculus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | optimal at 10 mM | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + activating transcription factor 2 | Mus musculus | ATF2 | ADP + phosphorylated activating transcription factor 2 | - |
? | |
| ATP + MAPKAP-K2 | Mus musculus | - |
ADP + phosphorylated MAPKAP-K2 | - |
? | |
| ATP + MAPKAP-K3 | Mus musculus | - |
ADP + phosphorylated MAPKAP-K3 | - |
? | |
| ATP + MEF2 | Mus musculus | - |
ADP + phosphorylated MEF2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
p38 MAPK isozyme alpha | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | native and recombinant p38 MAPKalpha is activated by phosphorylation at Thr180 and Tyr182 through recombinant GST-tagged MKK6b mutant S207E/T211E, for activation and specific dual phosphorylation of the recombinant enzyme | Mus musculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant GST-tagged p38 isozyme alpha from Escherichia coli strain BL21(DE3) by two steps of ion exchange chromatography to homogeneity, the recombinant enzyme is detagged | Mus musculus |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate | the kinetics of p38 MAPK follow a rapid-equilibrium random-order ternary-complex mechanism, the enzyme is highly specific for Ser-Pro or Thr-Pro motifs | Mus musculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + activating transcription factor 2 | ATF2 | Mus musculus | ADP + phosphorylated activating transcription factor 2 | - |
? | |
| ATP + activating transcription factor 2 | ATF2, recombinant GST-tagged ATF2DELTA115 | Mus musculus | ADP + phosphorylated activating transcription factor 2 | - |
? | |
| ATP + MAPKAP-K2 | - |
Mus musculus | ADP + phosphorylated MAPKAP-K2 | - |
? | |
| ATP + MAPKAP-K3 | - |
Mus musculus | ADP + phosphorylated MAPKAP-K3 | - |
? | |
| ATP + MEF2 | - |
Mus musculus | ADP + phosphorylated MEF2 | - |
? | |
| additional information | measurement of ATPase activity of p38 MAPK in an NADH-coupled assay | Mus musculus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| p38 MAP kinase alpha | - |
Mus musculus |
| p38 MAPKalpha | - |
Mus musculus |
| p38 mitogen-activated protein kinase alpha | - |
Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 27 | - |
assay at | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Mus musculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Mus musculus | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.000021 | - |
SB203580 | ATPase reaction versus ATP, pH 7.6, 27°C, recombinant p38 MAPK | Mus musculus | |
| 0.187 | - |
AMP-PCP | kinase reaction, pH 7.6, 27°C, recombinant p38 MAPK | Mus musculus | |
| 0.242 | - |
AMP-PCP | ATPase reaction versus ATP, pH 7.6, 27°C, recombinant p38 MAPK | Mus musculus | |
| 2 | - |
ADP | above, pH 7.6, 27°C, recombinant p38 MAPK | Mus musculus | |
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