Information on EC 2.7.3.4 - taurocyamine kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.3.4
-
RECOMMENDED NAME
GeneOntology No.
taurocyamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + taurocyamine = ADP + N-phosphotaurocyamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Taurine and hypotaurine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:taurocyamine N-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-72-6
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene CLF_107872
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene PHYSODRAFT_566100
UniProt
Manually annotated by BRENDA team
gene PHYSODRAFT_566100
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphocreatine
ATP + creatine
show the reaction diagram
-
low activity
-
-
?
ATP + arginine
ADP + ?
show the reaction diagram
2.9% of taurocyamine activity
-
-
?
ATP + beta-guanidinopropionic acid
?
show the reaction diagram
-
isoform PK1 shows 14% and isoform PK2 7% activity compared to tauromycine
-
-
?
ATP + D-lombricine
ADP + N-phospho-D-lombricine
show the reaction diagram
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
ATP + guanidopropionic acid
ADP + N-phosphoguanidinopropionic acid
show the reaction diagram
-
low activity
-
-
?
ATP + hypotaurocyamine
ADP + N-phosphohypotaurocyamine
show the reaction diagram
-
-
-
r
ATP + lombricine
ADP + N-phospholombricine
show the reaction diagram
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-lombricine
ADP + N-phospho-D-lombricine
show the reaction diagram
Q4AEC5, Q4AEC6
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chloroacetophenone
-
-
monoiodoacetate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
ADP
-
pH 7.2, 25°C
0.46 - 4.6
ATP
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5 - 22.59
ATP
1.4
glycocyamine
recombinant enzyme, pH 9.0, 30°C
4.5 - 94.1
Taurocyamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
glycocyamine
recombinant enzyme, pH 9.0, 30°C
58.67 - 180
Taurocyamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.855
lombricine
1.32
-
glycocyamine
2.541
-
lombricine
3.65
glycocyamine
4.04
taurocyamine
5.16
-
lombricine
10.4
taurocyamine
17.82
-
taurocyamine
28.71
-
taurocyamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
reaction with phosphotaurocyamine or hypophosphotaurocyamine
7.2
-
synthesis of ATP
8.5
-
reaction with hypotaurocyamine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8
-
pH 6.2: about 30% of maximal activity, pH 8.0: about 50% of maximal activity, synthesis of ATP
7.2 - 8.7
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pH 7.2: about 40% of maximal activity, pH 8.7: about 40% of maximal activity, synthesis of phosphotaurocyamine
7.7 - 9.5
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pH 7.7: about 50% of maximal activity, pH 9.5: about 70% of maximal activity, synthesis of phosphotaurocyamine; pH 7.7: about 60% of maximal activity, pH 9.5: about 60% of maximal activity, synthesis of hypophosphotaurocyamine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
-
20°C: 70% of maximal activity, 45°C: less than 45% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.39
sequence calculation, D2 domain
7.62
-
calculated
7.88
sequence calculation, full-length enzyme
7.9
-
calculated from amino acid sequence
8.09
sequence calculation, D1 domain
8.55
-
calculated
additional information
-
separation of 8 bands between pH 6.2 and pH 7.8 with taurocyamine kinase activity, the highest activity appears at pH 7.3
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
intra-uterine
Manually annotated by BRENDA team
a small part of the plume; a small part of the plume
Manually annotated by BRENDA team
oral and ventral suckers
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
UNIPROT
ORGANISM
Schistosoma mansoni;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39720
sequence calculation, D2 domain
40000
-
x * 40000, isoform PK1, SDS-PAGE
40570
sequence calculation, D1 domain
40830
calculated from amino acid sequence
41350
-
calculated from amino acid sequence
46200
-
calculated from amino acid sequence
59000
-
gel filtration
61000
-
ultracentrifugation
80220
-
calculated from amino acid sequence
80270
sequence calculation, full-length enzyme
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 40000, isoform PK1, SDS-PAGE; x * 80000, isoform PK2, SDS-PAGE
monomer
1 * 42000, SDS-PAGE, recombinant detagged D1 domain, SDS-PAGE, 1 * 80000, recombinant full-length enzyme, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
sitting-drop vapour-diffusion, 100 mM MES, pH 6.5, 25%(w/v) PEG 3000, 290 K, unit-cell parameters a = 52.7, b = 122.1, c = 63.2 A , beta = 108.5°, space group P21, 2.8 A resolution on ESRF beamline ID29
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
stable
642485
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol does not stabilize
-
structurally very unstable, gradual loss of enzyme activity even when it is stored on ice for several hours
unstable to freezing
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Unstable to lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, no decrease of activity when the crude extract is kept frozen for several months
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0°C, 0.033 M phosphate buffer, pH 7, or 0.05 M Tris-HCl buffer, pH 7.5, or 0.01 M glycylglycine buffer, pH 7, several weeks stable, or in 75% saturated ammonium sulfate solution, pH 8, stable for several months
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0°C, 0.1 M phosphate buffer, pH 7.2, saturated with mannitol, 0.02% NaN3, stable for more than 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatogrphy, concentrated to 10 mg ml-1 by lyophilization and resolubilized in MilliQ water, the purity is verified by the presence of a single band on overloaded Coomassie Blue-stained SDS-PAGE
amylose resin column chromatography, gel filtration
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recombinant enzyme coding region as maltose binding protein fusion protein from Escherichia coli strain TB1 by amylose affinity chromatography too homogeneity. Recombinant N-terminally GST-tagged enzyme D1 and D2 mutants from Escherichia coli strain BL21(DE3) pLysSby glutathione affinity chromatography, the GST-tag is cleaved off by thrombin treatment
recombinant N-terminal His6-PsPK protein from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant protein is purified by affinity chromatography using amylose resin
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recombinant protein is purified by affinity chromatography using amylose resin; recombinant protein is purified by affinity chromatography using amylose resin
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by Blue Sepharose affinity and anion exchange chromatography, followed by ultrafiltration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli TB1
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expressed in Escherichia coli TB1 cells
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expression in Escherichia coli TB1; expression in Escherichia coli TB1
gene CLF_107872, DNA and amino acid sequence determination and analysis, sequence comarisons and phylogenetic analysis, the coding region of the cDNA of D1D2 is cloned into the pMAL-c2 vector and expressed as maltose binding protein fusion protein in Escherichia coli strain TB1, quantitative real-time PCR enzyme expression analysis. Recombinant expression of N-terminally GST-tagged enzyme D1 and D2 mutants in Escherichia coli strain BL21(DE3) pLysS
gene PHYSODRAFT_566100, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of N-terminal His6-PsPK protein in Escherichia coli strain Rosetta 2 (DE3)
recombinant overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
sequence comparisons, recombinant expression of enzyme domain1 and domain2 mutants in Escherichia coli strain TB1
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the maltose binding protein-fused enzyme is expressed in Escherichia coli BL21(DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
H61A
site-directed mutagenesis of a domain 2 residue, the enzyme mutant shows altered kinetics and reduced activity compared to the wild-type enzyme; 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; 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; 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; 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; 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; 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; 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; site-directed mutagenesis of TKD1D2 in D2 region, the enzyme mutant shows altered kinetics and reduced activity 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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
Schistosoma mansoni is a trematode flatworm that has been identified as the aetiological agent of schistosomiasis, a disease that affects about 200 million people worldwide
pharmacology
the enzyme is a candidate chemotherapeutic target