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Literature summary for 2.7.12.1 extracted from
- Unveiling the novel dual specificity protein kinases in Bacillus anthracis (2012), J. Biol. Chem., 287, 26749-26763.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | PrkG activation by phosphorylation seems to be quite complex and is dependent on multiple residues, e.g. the two critical residues Tyr349 and Thr245 | Bacillus anthracis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| enzyme PrkD expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
| PrkG expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3) | Bacillus anthracis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K53M | site-directed mutagenesis, inactive mutant | Bacillus anthracis |
| additional information | loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation | Bacillus anthracis |
| T180A | site-directed mutagenesis, the mutant enzyme shows loss in activity | Bacillus anthracis |
| T181A | site-directed mutagenesis, the mutant enzyme shows loss in activity and in phosphorylation | Bacillus anthracis |
| T181A/Y182F | site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation | Bacillus anthracis |
| T245A/Y349F | site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation | Bacillus anthracis |
| Y182F | site-directed mutagenesis, the mutant enzyme shows loss in activity | Bacillus anthracis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| genistein | inhibits the enzyme and affects Bacillus anthracis cell growth | Bacillus anthracis |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required, the enzyme requires Mn2+ or Mg2+ for activity | Bacillus anthracis | |
| Mn2+ | required, the enzyme requires Mn2+ or Mg2+ for activity | Bacillus anthracis | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + a protein | Bacillus anthracis | - |
ADP + a phosphoprotein | - |
? | |
| additional information | Bacillus anthracis | PrkG is a unique dual specificity protein kinase that mediates autophosphorylation and substrate phosphorylation on Ser, Thr, and Tyr residues | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus anthracis | - |
several strains | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphorylation on Tyr residues regulates the kinase activity of PrkD. The enzyme is able to autophosphorylate on several Ser/Thr residues and three Tyr residues, e.g. Ser162, or Tyr182 and two probable phosphoresidues Thr180 and Thr181 that are present in the activation loop of the PrkD catalytic domain. Partial dephosphorylation occurs by PrpC, a Ser/Thr protein phosphatase, that is also found to possess dual specificity | Bacillus anthracis |
| phosphoprotein | phosphorylation on Tyr residues regulates the kinase activity of PrkG. The enzyme is able to autophosphorylate. Complete dephosphorylation occurs by PrpC, a Ser/Thr protein phosphatase, that is also found to possess dual specificity | Bacillus anthracis |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His- or GST-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel or glutathione affinity chromatography, respectively | Bacillus anthracis |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | the enzyme is expressed in all phases of growth | Bacillus anthracis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + a protein | - |
Bacillus anthracis | ADP + a phosphoprotein | - |
? | |
| ATP + myelin basic protein | the substrate is phosphorylated on Ser, Thr, and Tyr residues by PrkG | Bacillus anthracis | ADP + phospho-[myelin basic protein] | - |
? | |
| ATP + pyruvate kinase | phosphorylated by PrkD on Ser and Thr residues | Bacillus anthracis | ADP + phospho-[pyruvate kinase] | - |
? | |
| additional information | PrkG is a unique dual specificity protein kinase that mediates autophosphorylation and substrate phosphorylation on Ser, Thr, and Tyr residues | Bacillus anthracis | ? | - |
? | |
| additional information | no activity with pyruvate kinase as substrate, and with probable substrates Ef-Tu, Ef-G, SsbA, Bas4487, and Bas1176 | Bacillus anthracis | ? | - |
? | |
| additional information | the enzyme performs autophosphorylation on several Ser/Thr residues and three Tyr residues, e.g. Ser162 or Tyr182 and two probable phospho residues Thr180 and Thr181 that are present in the activation loop of the PrkD catalytic domain | Bacillus anthracis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Bas2037 | - |
Bacillus anthracis |
| Bas2152 | - |
Bacillus anthracis |
| DSPK | - |
Bacillus anthracis |
| dual specificity protein kinase | - |
Bacillus anthracis |
| PrkD | - |
Bacillus anthracis |
| PrkG | - |
Bacillus anthracis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
- |
Bacillus anthracis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Bacillus anthracis |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | dependent on | Bacillus anthracis | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | Ser/Thr protein kinases present in Bacillus anthracis genome: Bacillus anthracis has lost key tyrosine kinases and gained novel dual specificity kinases. Dual specificity protein kinases are identified, of which one is similar to the eukaryotic DYRK superfamily. PhrkD and PrkG DSPKs belong to different classes and have different modes of regulation. The mechanism of autophosphorylation and the substrate phosphorylation in PrkG is distinct from that of PrkD and involves Thr residues in addition to Tyr residues | Bacillus anthracis |
| malfunction | loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation | Bacillus anthracis |
| additional information | absence of characteristic DYRK motifs, such as the DYRK homology box, N-terminal autophosphorylation accessory region, and motif rich in Pro, Glu, Ser, and Thr residues (PEST) in PrkD | Bacillus anthracis |
| physiological function | possible role of the kinase in cell growth and development | Bacillus anthracis |
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