Information on EC 2.7.3.4 - taurocyamine kinase

Word Map on EC 2.7.3.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

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
-
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, 25C
0.46 - 4.6
ATP
6.1
glycocyamine
recombinant enzyme, pH 9.0, 30C
0.83
N-phosphotaurocyamine
-
pH 7.2, 25C
0.1
N-taurocyamine
-
pH 8.0, 25C
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
Phytophthora sojae
G5ADV1
recombinant enzyme, pH 9.0, 30C
4.5 - 94.1
Taurocyamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23
glycocyamine
Phytophthora sojae
G5ADV1
recombinant enzyme, pH 9.0, 30C
10661
58.67 - 180
Taurocyamine
1939
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.32
-
glycocyamine
2.541
-
lombricine
5.16
-
lombricine
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
-
pH 7.2: about 40% of maximal activity, pH 8.7: about 40% of maximal activity, synthesis of phosphotaurocyamine
7.7 - 9.5
-
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
-
20C: 70% of maximal activity, 45C: 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
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, 20C, 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
-
Unstable to lyophilization
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, no decrease of activity when the crude extract is kept frozen for several months
-
0C, 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
-
0C, 0.1 M phosphate buffer, pH 7.2, saturated with mannitol, 0.02% NaN3, stable for more than 2 months
-
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
-
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
-
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
-
expressed in Escherichia coli TB1 cells
-
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
-
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