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Literature summary extracted from

  • Tanaka, K.; Matsumoto, T.; Suzuki, T.
    Identification of amino acid residues responsible for taurocyamine binding in mitochondrial taurocyamine kinase from Arenicola brasiliensis (2011), Biochim. Biophys. Acta, 1814, 1219-1225.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.4 the maltose binding protein-fused enzyme is expressed in Escherichia coli BL21(DE3) cells Arenicola brasiliensis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.3.4 H67A the mutant shows a decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 H67A/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 K69A the mutant shows significantly increased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 K69A/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 K69R the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 K69R/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 K95A the mutant shows a 10fold increase in affinity for glycocyamine and has a 7.5fold higher catalytic efficiency for glycocyamine than the wild type enzyme Arenicola brasiliensis
2.7.3.4 K95E activity is largely lost in this mutant Arenicola brasiliensis
2.7.3.4 K95H the mutant has a 3fold higher affinity for taurocyamine Arenicola brasiliensis
2.7.3.4 K95I the mutant has a 3fold higher affinity for taurocyamine Arenicola brasiliensis
2.7.3.4 K95R the mutant has a 3fold higher affinity for taurocyamine Arenicola brasiliensis
2.7.3.4 K95Y an increase in substrate concentration causes a decrease in initial velocity of the reaction performed by this mutant (substrate inhibition) Arenicola brasiliensis
2.7.3.4 T68A the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 T68AA/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 T70A the mutant shows significantly increased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 T70A/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis
2.7.3.4 V71A the mutant shows significantly increased Km value compared to the wild type enzyme and acts like a glycocyamine kinase, rather than a tauromycine kinase Arenicola brasiliensis
2.7.3.4 V71A/K95Y the mutant shows significantly decreased Km value compared to the wild type enzyme Arenicola brasiliensis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.3.4 0.082
-
 Taurocyamine mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.14
-
 Taurocyamine mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.153
-
 Taurocyamine mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.184
-
 Taurocyamine mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.205
-
 Taurocyamine mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.217
-
 Taurocyamine mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.278
-
 Taurocyamine mutant enzyme K95I, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.287
-
 Taurocyamine mutant enzyme K95R, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.313
-
 Taurocyamine mutant enzyme K95H, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.332
-
 Taurocyamine mutant enzyme T70A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.603
-
 Taurocyamine mutant enzyme V71A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.718
-
 Taurocyamine mutant enzyme T68A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.742
-
 Taurocyamine mutant enzyme K69R, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.813
-
 Taurocyamine mutant enzyme H67A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 0.913
-
 Taurocyamine wild type enzyme, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 1.228
-
 Taurocyamine mutant enzyme K69A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 1.868
-
 Taurocyamine mutant enzyme T70A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 2.091
-
 Taurocyamine mutant enzyme V71A, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis
2.7.3.4 13.28
-
 Taurocyamine mutant enzyme K95E, in 100 mM Tris-HCl, at pH 8.0 and 25°C Arenicola brasiliensis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.3.4 mitochondrion
-
 Arenicola brasiliensis 5739
-

Organism

EC Number Organism UniProt Comment Textmining
2.7.3.4 Arenicola brasiliensis Q4AEC6
-
-

Substrates and Products (Substrate)

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