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Literature summary extracted from

  • Jarilla, B.R.; Tokuhiro, S.; Nagataki, M.; Uda, K.; Suzuki, T.; Acosta, L.P.; Agatsuma, T.
    The role of Y84 on domain 1 and Y87 on domain 2 of Paragonimus westermani taurocyamine kinase: insights on the substrate binding mechanism of a trematode phosphagen kinase (2013), Exp. Parasitol., 135, 695-700.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.3.4 sequence comparisons, recombinant expression of enzyme domain1 and domain2 mutants in Escherichia coli strain TB1 Paragonimus westermani

Protein Variants

EC Number Protein Variants Comment Organism
2.7.3.4 A59G site-directed mutagenesis on domain 1, the mutant shows a high decrease in affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 A62G site-directed mutagenesis on domain 2, inactive mutant Paragonimus westermani
2.7.3.4 G58R site-directed mutagenesis on domain 1, the mutant shows slightly decreased affinity for taurocyamine and a slightly increased activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 I60V site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 I63V site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 R61L site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 Y84E site-directed mutagenesis on domain 1, almost inactive mutant Paragonimus westermani
2.7.3.4 Y84H site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 Y84I site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme Paragonimus westermani
2.7.3.4 Y84R site-directed mutagenesis on domain 1, inactive mutant Paragonimus westermani
2.7.3.4 Y87E site-directed mutagenesis on domain 2, inactive mutant Paragonimus westermani
2.7.3.4 Y87H site-directed mutagenesis on domain 2, inactive mutant Paragonimus westermani
2.7.3.4 Y87I site-directed mutagenesis on domain 2, inactive mutant Paragonimus westermani
2.7.3.4 Y87R site-directed mutagenesis on domain 2, inactive mutant Paragonimus westermani

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.3.4 Mg2+ required Paragonimus westermani

Natural Substrates/ Products (Substrates)

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

Organism

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

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
-
 ?
2.7.3.4 ATP + taurocyamine the enzyme has a unique substrate binding mechanism Paragonimus westermani ADP + N-phosphotaurocyamine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.3.4 More the enzyme contains two domains, domain 1 and domain 2. The two domains function independently Paragonimus westermani

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.3.4 ATP
-
 Paragonimus westermani

General Information

EC Number General Information Comment Organism
2.7.3.4 additional information the residues Y84 and Y87 of domains 1 and 2, respetively are required for catalytic activity, while the residues A59 and A62 in the GS region of domains 1 and 2, respectively, have a key role in substrate binding Paragonimus westermani