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Literature summary for 2.7.3.4 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
Search for more literature for 2.7.3.4

Cloned(Commentary)

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Paragonimus westermani C7BCG0
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Paragonimus westermani

pI Value

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

kcat/KM [mM/s]

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