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ADP + phosphocreatine
ATP + creatine
-
low activity
-
-
?
ATP + arginine
ADP + ?
2.9% of taurocyamine activity
-
-
?
ATP + beta-guanidinopropionic acid
?
-
isoform PK1 shows 14% and isoform PK2 7% activity compared to tauromycine
-
-
?
ATP + D-lombricine
ADP + N-phospho-D-lombricine
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
ATP + guanidopropionic acid
ADP + N-phosphoguanidinopropionic acid
-
low activity
-
-
?
ATP + hypotaurocyamine
ADP + N-phosphohypotaurocyamine
-
-
-
r
ATP + lombricine
ADP + N-phospholombricine
ATP + taurocyamine
ADP + N-phosphotaurocyamine
additional information
?
-
ATP + glycocyamine
ADP + N-phosphoglycocyamine
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
no activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
7% of taurocyamine activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
-
low activity
-
r
ATP + glycocyamine
ADP + N-phosphoglycocyamine
low activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
low activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
no activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
35% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
30% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
9% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
-
low activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
21% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
31% of taurocyamine activity
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
high substrate specificity for taurocyamine
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
the enzyme has a unique substrate binding mechanism
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
strong activity
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
the enzyme catalyzes the reversibleMg2-dependent transfer of a phosphoryl group between ATP and taurocyamine
-
-
r
additional information
?
-
cytoplasmic TK shows activity only for D-lombricine and taurocyamine (the second activity being in the range of 15% to that for the main substrate), no activity for creatine
-
-
?
additional information
?
-
cytoplasmic TK shows activity only for D-lombricine and taurocyamine (the second activity being in the range of 15% to that for the main substrate), no activity for creatine
-
-
?
additional information
?
-
no activity for creatine
-
-
?
additional information
?
-
no activity for creatine
-
-
?
additional information
?
-
the mitochondrial isoform of MiTK shows high activity for glycocyamine (48%), in addition to D-lombricine (80%), the MiTK also shows weak but significant activity for L-arginine (0.2%)
-
-
?
additional information
?
-
the mitochondrial isoform of MiTK shows high activity for glycocyamine (48%), in addition to D-lombricine (80%), the MiTK also shows weak but significant activity for L-arginine (0.2%)
-
-
?
additional information
?
-
residues R58, I60 and Y84 of domain 1, and H60, I63 and Y87 of domain 2 participate in binding taurocyamine. Recombinant CsTK enzyme protein has low sensitivity and specificity toward Clonorchis sinensis and platyhelminth-infected human sera on ELISA
-
-
?
additional information
?
-
-
residues R58, I60 and Y84 of domain 1, and H60, I63 and Y87 of domain 2 participate in binding taurocyamine. Recombinant CsTK enzyme protein has low sensitivity and specificity toward Clonorchis sinensis and platyhelminth-infected human sera on ELISA
-
-
?
additional information
?
-
-
no activity with L-arginine, D-arginine, creatine, glycocyamine, gamma-guanidinobutyric acid, homoarginine, methylguanidine and L-acetylguanidine
-
-
?
additional information
?
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
additional information
?
-
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
additional information
?
-
no kinase activity with the more ubiquitous guanidinium substrates, creatine or arginine
-
-
?
additional information
?
-
-
no kinase activity with the more ubiquitous guanidinium substrates, creatine or arginine
-
-
?
additional information
?
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
additional information
?
-
no kinase activity with the more ubiquitous guanidinium substrates, creatine or arginine
-
-
?
additional information
?
-
recombinant enzyme shows catalytic activity with several guanidylic compounds, the highest activity being measured with taurocyamine, taurocyamine may not be the physiological substrate and that Schistosoma mansoni may use another phosphagen
-
-
?
additional information
?
-
-
recombinant enzyme shows catalytic activity with several guanidylic compounds, the highest activity being measured with taurocyamine, taurocyamine may not be the physiological substrate and that Schistosoma mansoni may use another phosphagen
-
-
?
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ATP + D-lombricine
ADP + N-phospho-D-lombricine
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
ATP + taurocyamine
ADP + N-phosphotaurocyamine
additional information
?
-
ATP + glycocyamine
ADP + N-phosphoglycocyamine
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
low activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
low activity
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
-
-
-
r
additional information
?
-
cytoplasmic TK shows activity only for D-lombricine and taurocyamine (the second activity being in the range of 15% to that for the main substrate), no activity for creatine
-
-
?
additional information
?
-
cytoplasmic TK shows activity only for D-lombricine and taurocyamine (the second activity being in the range of 15% to that for the main substrate), no activity for creatine
-
-
?
additional information
?
-
no activity for creatine
-
-
?
additional information
?
-
no activity for creatine
-
-
?
additional information
?
-
the mitochondrial isoform of MiTK shows high activity for glycocyamine (48%), in addition to D-lombricine (80%), the MiTK also shows weak but significant activity for L-arginine (0.2%)
-
-
?
additional information
?
-
the mitochondrial isoform of MiTK shows high activity for glycocyamine (48%), in addition to D-lombricine (80%), the MiTK also shows weak but significant activity for L-arginine (0.2%)
-
-
?
additional information
?
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
additional information
?
-
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
additional information
?
-
the phosphagen kinases in the invertebrates are observed to utilize other guanidino substrates. These include arginine, glycocyamine, taurocyamine, lombricine, hypotaurocyamine, and opheline. Analysis of phosphagen formation by 31P NMR, overview
-
-
?
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6.1
glycocyamine
recombinant enzyme, pH 9.0, 30°C
0.83
N-phosphotaurocyamine
-
pH 7.2, 25°C
0.1
N-taurocyamine
-
pH 8.0, 25°C
0.082 - 33.44
Taurocyamine
additional information
additional information
-
0.46
ATP
recombinant domain D1, pH 8.0, 25°C
0.75
ATP
recombinant domain D2, pH 8.0, 25°C
0.78
ATP
recombinant full-length enzyme, pH 8.0, 25°C
1.8
ATP
recombinant enzyme, pH 9.0, 30°C, with taurocyamine
4.6
ATP
recombinant enzyme, pH 9.0, 30°C, with glycocyamine
0.082
Taurocyamine
mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.14
Taurocyamine
mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.153
Taurocyamine
mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.184
Taurocyamine
mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.205
Taurocyamine
mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.217
Taurocyamine
mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.269
Taurocyamine
-
isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.278
Taurocyamine
mutant enzyme K95I, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.287
Taurocyamine
mutant enzyme K95R, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.313
Taurocyamine
mutant enzyme K95H, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.332
Taurocyamine
mutant enzyme T70A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.35
Taurocyamine
recombinant domain D1, pH 8.0, 25°C
0.48
Taurocyamine
recombinant domain D2, pH 8.0, 25°C
0.49
Taurocyamine
recombinant full-length enzyme, pH 8.0, 25°C
0.52
Taurocyamine
recombinant enzyme, pH 9.0, 30°C
0.603
Taurocyamine
mutant enzyme V71A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.718
Taurocyamine
mutant enzyme T68A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.742
Taurocyamine
mutant enzyme K69R, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.813
Taurocyamine
mutant enzyme H67A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.913
Taurocyamine
wild type enzyme, in 100 mM Tris-HCl, at pH 8.0 and 25°C
0.969
Taurocyamine
-
isoform PK2, in 100 mM Tris-HCl, at pH 8.0 and 25°C
1.228
Taurocyamine
mutant enzyme K69A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
1.868
Taurocyamine
mutant enzyme T70A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
2.091
Taurocyamine
mutant enzyme V71A, in 100 mM Tris-HCl, at pH 8.0 and 25°C
13.28
Taurocyamine
mutant enzyme K95E, in 100 mM Tris-HCl, at pH 8.0 and 25°C
additional information
additional information
comparisons of wild-type and mutant enzyme kinetics, overview
-
additional information
additional information
-
comparisons of wild-type and mutant enzyme kinetics, overview
-
additional information
additional information
steady-state kinetic analysis, overview. Analysis of quaternary structure and cooperativity in ligand-binding by ITC: absence of inter-subunit cooperativity in forming the PsTKTSAC
-
additional information
additional information
-
steady-state kinetic analysis, overview. Analysis of quaternary structure and cooperativity in ligand-binding by ITC: absence of inter-subunit cooperativity in forming the PsTKTSAC
-
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evolution
the enzyme belongs to the highly conserved phosphagen (PK) kinase family of enzymes. The polypeptide is homologous to taurocyamine kinase (TK) of the invertebrate animals and consists of two contiguous domains. Clonorchis sinensis CsTK gene consists of 13 exons intercalated with 12 introns. This suggests an evolutionary pathway originating from an arginine kinase gene group, and distinguishes annelid taurocyamine kinase from the general creatine kinase phylogenetic group
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
evolution
the enzyme belongs to the phosphagen kinases family of enzymes. Phylogenetic analysis of oomycete enzymes, overview
evolution
-
the enzyme belongs to the phosphagen kinases family of enzymes. Phylogenetic analysis of oomycete enzymes, overview
-
physiological function
within animal species, these enzymes play a critical role in energy homeostasis by catalyzing the reversible transfer of a high-energy phosphoryl group from Mg-ATP to an acceptor molecule containing a guanidinium group
physiological function
-
within animal species, these enzymes play a critical role in energy homeostasis by catalyzing the reversible transfer of a high-energy phosphoryl group from Mg-ATP to an acceptor molecule containing a guanidinium group
-
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
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
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monomer
1 * 42000, SDS-PAGE, recombinant detagged D1 domain, SDS-PAGE, 1 * 80000, recombinant full-length enzyme, SDS-PAGE
?
-
x * 40000, isoform PK1, SDS-PAGE
?
-
x * 80000, isoform PK2, SDS-PAGE
dimer
2 + 51000, about, sequence calculation, the enzyme is dimeric but lacks cooperativity between the subunits in forming a transition state analogue complex
dimer
-
2 + 51000, about, sequence calculation, the enzyme is dimeric but lacks cooperativity between the subunits in forming a transition state analogue complex
-
additional information
-
SDS-PAGE reveals 3 protein bands: 11000 Da, 13000-14000 Da and 21000-22000 Da
additional information
the enzyme contains two domains, domain 1 and domain 2. The two domains function independently
additional information
-
the enzyme contains two domains, domain 1 and domain 2. The two domains function independently
additional information
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
additional information
-
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
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H67A
the mutant shows a decreased Km value compared to the wild type enzyme
H67A/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
K69A
the mutant shows significantly increased Km value compared to the wild type enzyme
K69A/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
K69R
the mutant shows significantly decreased Km value compared to the wild type enzyme
K69R/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
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
K95E
activity is largely lost in this mutant
K95H
the mutant has a 3fold higher affinity for taurocyamine
K95I
the mutant has a 3fold higher affinity for taurocyamine
K95R
the mutant has a 3fold higher affinity for taurocyamine
K95Y
an increase in substrate concentration causes a decrease in initial velocity of the reaction performed by this mutant (substrate inhibition)
T68A
the mutant shows significantly decreased Km value compared to the wild type enzyme
T68AA/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
T70A
the mutant shows significantly increased Km value compared to the wild type enzyme
T70A/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
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
V71A/K95Y
the mutant shows significantly decreased Km value compared to the wild type enzyme
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
A62G
site-directed mutagenesis on domain 2, inactive mutant
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
I60V
site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme
I63V
site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme
R61L
site-directed mutagenesis on domain 2, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme
Y84E
site-directed mutagenesis on domain 1, almost inactive mutant
Y84H
site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme
Y84I
site-directed mutagenesis on domain 1, the mutant shows decreased affinity and activity for taurocyamine compared to the wild-type enzyme
Y84R
site-directed mutagenesis on domain 1, inactive mutant
Y87E
site-directed mutagenesis on domain 2, inactive mutant
Y87H
site-directed mutagenesis on domain 2, inactive mutant
Y87I
site-directed mutagenesis on domain 2, inactive mutant
Y87R
site-directed mutagenesis on domain 2, inactive mutant
C268S
site-directed mutagenesis
C268S/C631S
site-directed mutagenesis
C631S
site-directed mutagenesis
H61A
site-directed mutagenesis of a domain 2 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
H61A
site-directed mutagenesis of TKD1D2 in D2 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
I60A
site-directed mutagenesis of a domain 1 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
I60A
site-directed mutagenesis of TKD1D2 in D1 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
I63A
site-directed mutagenesis of a domain 2 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
I63A
site-directed mutagenesis of TKD1D2 in D2 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R58A
site-directed mutagenesis of a domain 1 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
R58A
site-directed mutagenesis of TKD1D2 in D1 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y84A
site-directed mutagenesis of a domain 1 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y84A
site-directed mutagenesis of TKD1D2 in D1 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y84R
site-directed mutagenesis of a domain 1 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y84R
site-directed mutagenesis of TKD1D2 in D1 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y87A
site-directed mutagenesis of a domain 2 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y87A
site-directed mutagenesis of TKD1D2 in D2 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y87R
site-directed mutagenesis of a domain 2 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
Y87R
site-directed mutagenesis of TKD1D2 in D2 region, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme
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Surholt, B.
Taurocyamine kinase from body-wall musculature of the lugworm Arenicola marina
Eur. J. Biochem.
93
279-285
1979
Arenicola marina
brenda
Kassab, R.; Pradel, L.A.; van Thoai, N.
ATP:taurocyamine and ATP:lombricine phosphotransferases. Purification and study of SH groups
Biochim. Biophys. Acta
99
397-405
1965
Arenicola marina
brenda
van Thoai, N.; Robin, Y.; Pradel, L.A.
Hypotaurocyamine phosphokinase comparaison avec la taurocyamine phosphokinase
Biochim. Biophys. Acta
73
437-444
1963
Arenicola marina
brenda
Uda, K.; Saishoji, N.; Ichinari, S.; Ellington, W.R.; Suzuki, T.
Origin and properties of cytoplasmic and mitochondrial isoforms of taurocyamine kinase
FEBS J.
272
3521-3530
2005
Arenicola brasiliensis (Q4AEC5), Arenicola brasiliensis (Q4AEC6), Arenicola brasiliensis
brenda
Uda, K.; Tanaka, K.; Bailly, X.; Zal, F.; Suzuki, T.
Phosphagen kinase of the giant tubeworm Riftia pachyptila. Cloning and expression of cytoplasmic and mitochondrial isoforms of taurocyamine kinase
Int. J. Biol. Macromol.
37
54-60
2005
Arenicola brasiliensis, Riftia pachyptila (Q4AEC7), Riftia pachyptila (Q4AEC8), Riftia pachyptila
brenda
Tanaka, K.; Uda, K.; Shimada, M.; Takahashi, K.I.; Gamou, S.; Ellington, W.R.; Suzuki, T.
Evolution of the cytoplasmic and mitochondrial phosphagen kinases unique to annelid groups
J. Mol. Evol.
65
616-625
2007
Arenicola brasiliensis, Arenicola brasiliensis (Q4AEC5)
brenda
Awama, A.M.; Paracuellos, P.; Laurent, S.; Dissous, C.; Marcillat, O.; Gouet, P.
Crystallization and x-ray analysis of the Schistosoma mansoni guanidino kinase
Acta Crystallogr. Sect. F
F64
854-857
2008
Schistosoma mansoni (P16641), Schistosoma mansoni
brenda
Suzuki, T.; Uda, K.; Adachi, M.; Sanada, H.; Tanaka, K.; Mizuta, C.; Ishida, K.; Ellington, W.R.
Evolution of the diverse array of phosphagen systems present in annelids
Comp. Biochem. Physiol. B
152
60-66
2008
Arenicola brasiliensis (Q4AEC5), Arenicola brasiliensis (Q4AEC6)
brenda
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
FEBS Lett.
583
2218-2224
2009
Paragonimus westermani (C7BCG0), Paragonimus westermani
brenda
Uda, K.; Kuwasaki, A.; Shima, K.; Matsumoto, T.; Suzuki, T.
The role of Arg-96 in Danio rerio creatine kinase in substrate recognition and active center configuration
Int. J. Biol. Macromol.
44
413-418
2009
Danio rerio
brenda
Tanaka, K.; Matsumoto, T.; Suzuki, T.
Identification of amino acid residues responsible for taurocyamine binding in mitochondrial taurocyamine kinase from Arenicola brasiliensis
Biochim. Biophys. Acta
1814
1219-1225
2011
Arenicola brasiliensis (Q4AEC6), Arenicola brasiliensis
brenda
Uda, K.; Hoshijima, M.; Suzuki, T.
A novel taurocyamine kinase found in the protist Phytophthora infestans
Comp. Biochem. Physiol. B
165
42-48
2013
Phytophthora infestans
brenda
Palmer, A.; Begres, B.N.; Van Houten, J.M.; Snider, M.J.; Fraga, D.
Characterization of a putative oomycete taurocyamine kinase: implications for the evolution of the phosphagen kinase family
Comp. Biochem. Physiol. B
166
173-181
2013
Phytophthora sojae (G5ADV1), Phytophthora sojae, Phytophthora sojae P6497 (G5ADV1)
brenda
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
Exp. Parasitol.
135
695-700
2013
Paragonimus westermani (C7BCG0), Paragonimus westermani
brenda
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
J. Biol. Chem.
290
12951-12963
2015
Schistosoma mansoni (P16641), Schistosoma mansoni
brenda
Xiao, J.Y.; Lee, J.Y.; Tokuhiro, S.; Nagataki, M.; Jarilla, B.R.; Nomura, H.; Kim, T.I.; Hong, S.J.; Agatsuma, T.
Molecular cloning and characterization of taurocyamine kinase from Clonorchis sinensis: a candidate chemotherapeutic target
PLoS Negl. Trop. Dis.
7
e2548
2013
Clonorchis sinensis (G7YHA8), Clonorchis sinensis
brenda
Saijuntha, W.; Tantrawatpan, C.; Jarilla, B.R.; Agatsuma, T.; Andrews, R.H.; Petney, T.N.
Intron sequence of the taurocyamine kinase gene as a marker to investigate genetic variation of Paragonimus species in Japan and the origins of triploidy in P. westermani
Trans. R. Soc. Trop. Med. Hyg.
110
67-73
2016
Paragonimus westermani, Paragonimus skrjabini miyazakii, Paragonimus ohirai, Paragonimus iloktsuenensis
brenda