Literature summary extracted from
Merceron, R.; Awama, A.M.; Montserret, R.; Marcillat, O.; Gouet, P.
The substrate-free and -bound crystal structures of the duplicated taurocyamine kinase from the human parasite Schistosoma mansoni (2015), J. Biol. Chem., 290, 12951-12963.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.3.4 |
recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha |
Schistosoma mansoni |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.3.4 |
purified recombinant wild-type and mutant enzymes complexed with taurocyamine or L-arginine, sitting drop vapor diffusion method, mixing of 5 mg/ml protein in 20mM Tris-HCl, pH 8.5, with reservoir solution, containing 200mM diammonium tartrate, pH 5.4, 20% w/v PEG 3350, 20% v/v ethylene glycol, in a 2:1 or 1:1 protein/solution volume ratio, 2 weeks, 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution leads to a small angle x-ray scattering model of SmTK-TSA in solution with two closed active sites, molecular replacement. The SmTK crystal is soaked with the dead end transition state analogue components taurocyamine-NO3 2-MgADP |
Schistosoma mansoni |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.3.4 |
C268S |
site-directed mutagenesis |
Schistosoma mansoni |
2.7.3.4 |
C268S/C631S |
site-directed mutagenesis |
Schistosoma mansoni |
2.7.3.4 |
C631S |
site-directed mutagenesis |
Schistosoma mansoni |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.3.4 |
Mg2+ |
dependent on |
Schistosoma mansoni |
|
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 |
Schistosoma mansoni |
- |
ADP + N-phosphotaurocyamine |
- |
r |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.3.4 |
Schistosoma mansoni |
P16641 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.3.4 |
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by Blue Sepharose affinity and anion exchange chromatography, followed by ultrafiltration |
Schistosoma mansoni |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.7.3.4 |
ATP + taurocyamine = ADP + N-phosphotaurocyamine |
an arginine residue of the phosphagen specificity loop is crucial for substrate specificity, mechanism and structure-function relationship, overview |
Schistosoma mansoni |
|
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 |
- |
Schistosoma mansoni |
ADP + N-phosphotaurocyamine |
- |
r |
|
2.7.3.4 |
ATP + taurocyamine |
the enzyme catalyzes the reversibleMg2-dependent transfer of a phosphoryl group between ATP and taurocyamine |
Schistosoma mansoni |
ADP + N-phosphotaurocyamine |
- |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.7.3.4 |
More |
the two unliganded lobes present a canonical open conformation and interact via their respective C- and N-terminal domains at a helix-mediated interface. The two lobes function independently |
Schistosoma mansoni |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.3.4 |
ADP |
- |
Schistosoma mansoni |
|
2.7.3.4 |
ATP |
- |
Schistosoma mansoni |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.3.4 |
evolution |
the enzyme belongs to the phosphagen kinase (PK) family. Schistosoma mansoni taurocyamine SmTK is derived from gene duplication, as are all known trematode taurocyamine kinases |
Schistosoma mansoni |