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Literature summary extracted from

  • Arora, G.; Sajid, A.; Arulanandh, M.D.; Singhal, A.; Mattoo, A.R.; Pomerantsev, A.P.; Leppla, S.H.; Maiti, S.; Singh, Y.
    Unveiling the novel dual specificity protein kinases in Bacillus anthracis (2012), J. Biol. Chem., 287, 26749-26763.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.12.1 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)

EC Number Cloned (Comment) Organism
2.7.12.1 enzyme PrkD expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus anthracis
2.7.12.1 PrkG expression analysis, recombinant expression of His- or GST-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus anthracis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.12.1 K53M site-directed mutagenesis, inactive mutant Bacillus anthracis
2.7.12.1 additional information loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation Bacillus anthracis
2.7.12.1 T180A site-directed mutagenesis, the mutant enzyme shows loss in activity Bacillus anthracis
2.7.12.1 T181A site-directed mutagenesis, the mutant enzyme shows loss in activity and in phosphorylation Bacillus anthracis
2.7.12.1 T181A/Y182F site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation Bacillus anthracis
2.7.12.1 T245A/Y349F site-directed mutagenesis, the mutant enzyme shows high loss in activity and in phosphorylation Bacillus anthracis
2.7.12.1 Y182F site-directed mutagenesis, the mutant enzyme shows loss in activity Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.12.1 genistein inhibits the enzyme and affects Bacillus anthracis cell growth Bacillus anthracis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.12.1 Mg2+ required, the enzyme requires Mn2+ or Mg2+ for activity Bacillus anthracis
2.7.12.1 Mn2+ required, the enzyme requires Mn2+ or Mg2+ for activity Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.12.1 ATP + a protein Bacillus anthracis
-
 ADP + a phosphoprotein
-
 ?
2.7.12.1 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

EC Number Organism UniProt Comment Textmining
2.7.12.1 Bacillus anthracis
-
 several strains
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.12.1 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
2.7.12.1 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)

EC Number Purification (Comment) Organism
2.7.12.1 recombinant His- or GST-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel or glutathione affinity chromatography, respectively Bacillus anthracis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.12.1 additional information the enzyme is expressed in all phases of growth Bacillus anthracis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.12.1 ATP + a protein
-
 Bacillus anthracis ADP + a phosphoprotein
-
 ?
2.7.12.1 ATP + myelin basic protein the substrate is phosphorylated on Ser, Thr, and Tyr residues by PrkG Bacillus anthracis ADP + phospho-[myelin basic protein]
-
 ?
2.7.12.1 ATP + pyruvate kinase phosphorylated by PrkD on Ser and Thr residues Bacillus anthracis ADP + phospho-[pyruvate kinase]
-
 ?
2.7.12.1 additional information PrkG is a unique dual specificity protein kinase that mediates autophosphorylation and substrate phosphorylation on Ser, Thr, and Tyr residues Bacillus anthracis ?
-
 ?
2.7.12.1 additional information no activity with pyruvate kinase as substrate, and with probable substrates Ef-Tu, Ef-G, SsbA, Bas4487, and Bas1176 Bacillus anthracis ?
-
 ?
2.7.12.1 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

EC Number Synonyms Comment Organism
2.7.12.1 Bas2037
-
 Bacillus anthracis
2.7.12.1 Bas2152
-
 Bacillus anthracis
2.7.12.1 DSPK
-
 Bacillus anthracis
2.7.12.1 dual specificity protein kinase
-
 Bacillus anthracis
2.7.12.1 PrkD
-
 Bacillus anthracis
2.7.12.1 PrkG
-
 Bacillus anthracis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.12.1 25
-
-
 Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.12.1 7.2
-
 assay at Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.12.1 ATP dependent on Bacillus anthracis

General Information

EC Number General Information Comment Organism
2.7.12.1 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
2.7.12.1 malfunction loss of Ser162 and Tyr182 in PrkD results in a significant loss in substrate phosphorylation Bacillus anthracis
2.7.12.1 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
2.7.12.1 physiological function possible role of the kinase in cell growth and development Bacillus anthracis