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Literature summary extracted from

  • Jarilla, B.R.; Tokuhiro, S.; Nagataki, M.; Hong, S.J.; Uda, K.; Suzuki, T.; Agatsuma, T.
    Molecular characterization and kinetic properties of a novel two-domain taurocyamine kinase from the lung fluke Paragonimus westermani (2009), FEBS Lett., 583, 2218-2224.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.4 expressed in Escherichia coli TB1 cells Paragonimus westermani

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.4 0.57
-
 Taurocyamine
-
 Paragonimus westermani
2.7.3.4 0.98
-
 ATP
-
 Paragonimus westermani
2.7.3.4 33.44
-
 Taurocyamine
-
 Paragonimus westermani

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.3.4 80220
-
 calculated from amino acid sequence Paragonimus westermani

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.4 Paragonimus westermani C7BCG0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.3.4 amylose resin column chromatography, gel filtration Paragonimus westermani

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.3.4 ATP + taurocyamine
-
 Paragonimus westermani ADP + N-phosphotaurocyamine
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.3.4 ATP
-
 Paragonimus westermani

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.3.4 Paragonimus westermani calculated from amino acid sequence
-
 7.9

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.3.4 58.67
-
 Taurocyamine
-
 Paragonimus westermani