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Literature summary for 2.7.14.1 extracted from

  • Jung, H.; Choi, Y.; Lee, D.; Seo, J.K.; Kee, J.M.
    Distinct phosphorylation and dephosphorylation dynamics of protein arginine kinases revealed by fluorescent activity probes (2019), Chem. Commun. (Camb.), 55, 7482-7485 .
    View publication on PubMed
Search for more literature for 2.7.14.1

Application

Application Comment Organism
analysis reversible fluorescent activity probes for protein Arg kinases and phosphatases to allow real-time kinetic assays, probe is based on the chelation-enhanced fluorescence (CHEF) effect of the cysteine-sulfonamido-oxine fluorophore Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + a [protein]-Nomega-phospho-L-arginine Geobacillus stearothermophilus the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP ATP + a [protein]-L-arginine
-
 r
ATP + a [protein]-L-arginine Geobacillus stearothermophilus the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP ADP + a [protein]-Nomega-phospho-L-arginine
-
 r

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus P0DMM5
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + a [protein]-Nomega-phospho-L-arginine
-
 Geobacillus stearothermophilus ATP + a [protein]-L-arginine
-
 r
ADP + a [protein]-Nomega-phospho-L-arginine the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP Geobacillus stearothermophilus ATP + a [protein]-L-arginine
-
 r
ADP + [Ac-KIVQSKRGGGGYIK-NH2]-Nomega-phospho-L-arginine peptide substrate derived from the CtsR protein Geobacillus stearothermophilus ATP + [Ac-KIVQSKRGGGGYIK-NH2]-L-arginine
-
 r
ATP + a [protein]-L-arginine
-
 Geobacillus stearothermophilus ADP + a [protein]-Nomega-phospho-L-arginine
-
 r
ATP + a [protein]-L-arginine the enzyme can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase. The enzyme can also mediate the dephosphorylation of the pArg residue to generate ATP Geobacillus stearothermophilus ADP + a [protein]-Nomega-phospho-L-arginine
-
 r

Synonyms

Synonyms Comment Organism
McsB
-
 Geobacillus stearothermophilus
protein Arg kinase McsB
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 Geobacillus stearothermophilus

General Information

General Information Comment Organism
physiological function protein arginine phosphorylation regulates stress responses and virulence in bacteria. It can dephosphorylate phosphoarginine residues to produce ATP from ADP, implicating the dynamic control of protein pArg levels by the kinase even without a phosphatase Geobacillus stearothermophilus