Literature summary for 2.7.3.4 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.

Search for more literature for 2.7.3.4

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
A62G	site-directed mutagenesis on domain 2, inactive mutant	Paragonimus westermani
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
I60V	site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme	Paragonimus westermani
I63V	site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme	Paragonimus westermani
R61L	site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme	Paragonimus westermani
Y84E	site-directed mutagenesis on domain 1, almost inactive mutant	Paragonimus westermani
Y84H	site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme	Paragonimus westermani
Y84I	site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme	Paragonimus westermani
Y84R	site-directed mutagenesis on domain 1, inactive mutant	Paragonimus westermani
Y87E	site-directed mutagenesis on domain 2, inactive mutant	Paragonimus westermani
Y87H	site-directed mutagenesis on domain 2, inactive mutant	Paragonimus westermani
Y87I	site-directed mutagenesis on domain 2, inactive mutant	Paragonimus westermani
Y87R	site-directed mutagenesis on domain 2, inactive mutant	Paragonimus westermani

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Paragonimus westermani

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Paragonimus westermani	C7BCG0	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + taurocyamine	-	Paragonimus westermani	ADP + N-phosphotaurocyamine	-	?
ATP + taurocyamine	the enzyme has a unique substrate binding mechanism	Paragonimus westermani	ADP + N-phosphotaurocyamine	-	?

Subunits

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Paragonimus westermani

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)