Information on EC 2.7.3.4 - taurocyamine kinase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
2.7.3.4
-
RECOMMENDED NAME
GeneOntology No.
taurocyamine kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + taurocyamine = ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
phospho group transfer
-
-
phospho group transfer
Q4AEC7, Q4AEC8, -
;
phospho group transfer
-
;
PATHWAY
KEGG Link
MetaCyc Link
Taurine and hypotaurine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
ATP:taurocyamine N-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP:taurocyamine phosphotransferase
-
-
-
-
guanidino kinase
-
-
kinase (phosphorylating), taurocyamine
-
-
-
-
kinase, taurocyamine (phosphorylating)
-
-
-
-
phosphagen kinase
Q4AEC7, Q4AEC8
-
taurocyamine kinase
-
-
taurocyamine kinase
Q4AEC5, Q4AEC6
-
taurocyamine kinase
Q4AEC7, Q4AEC8
-
taurocyamine phosphotransferase
-
-
-
-
TK
-
cytoplasmic enzyme
TK
Q4AEC5, Q4AEC6
-
TPK
-
-
-
-
MiTK
Q4AEC5
mitochondrial enzyme
additional information
-
the K95Y mutant of lombricine kinase functions as taurocyamine kinase
CAS REGISTRY NUMBER
COMMENTARY
9026-72-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
recombinant enzyme
SwissProt
Manually annotated by BRENDA team
rekombinant enzyme
SwissProt
Manually annotated by BRENDA team
cercariae, Puerto Rican strain, cloned into a pET21 plasmid without any tag, expression in Escherichia coli BL21 (DE3)
Uniprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q4AEC7, Q4AEC8, -
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
Q4AEC5, Q4AEC6
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
Q4AEC5, Q4AEC6
-
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
no activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
Q4AEC7, Q4AEC8, -
no activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
-
low activity
-
r
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
Q4AEC7, Q4AEC8, -
35% of taurocyamine activity
-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
7% of taurocyamine activity
-
-
?
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
-
low activity
-
-
-
ATP + lombricine
ADP + N-phospholombricine
show the reaction diagram
Q4AEC7, Q4AEC8, -
21% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
show the reaction diagram
-, Q4AEC5, Q4AEC6
30% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
show the reaction diagram
Q4AEC7, Q4AEC8, -
31% of taurocyamine activity
-
-
?
ATP + lombricine
ADP + N-phospholombricine
show the reaction diagram
-, Q4AEC5, Q4AEC6
9% of taurocyamine activity
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
-
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AEC5, Q4AEC6
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AEC7, Q4AEC8, -
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
C7BCG0
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AEC7, Q4AEC8, -
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
strong activity
-
-
?
additional information
?
-
Q4AEC5, Q4AEC6
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
?
-
Q4AEC5, Q4AEC6
no activity for creatine
-
-
-
additional information
?
-
Q4AEC5, Q4AEC6
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
?
-
P16641, -
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
?
-
-
no activity with L-arginine, D-arginine, creatine, glycocyamine, gamma-guanidinobutyric acid, homoarginine, methylguanidine and L-acetylguanidine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Q4AEC5, Q4AEC6
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AEC5, Q4AEC6
-
-
-
r
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-, Q4AEC5, Q4AEC6
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
Q4AEC7, Q4AEC8, -
key role in the interconnection between energy production and utilization in animals
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
-
key role in the interconnection between energy production and utilization in animals
-
-
?
additional information
?
-
Q4AEC5, Q4AEC6
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
?
-
Q4AEC5, Q4AEC6
no activity for creatine
-
-
-
additional information
?
-
Q4AEC5, Q4AEC6
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%)
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
required, maximal activity at 10 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Chloroacetophenone
-
-
monoiodoacetate
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.2
-
ADP
-
pH 7.2, 25C
0.98
-
ATP
C7BCG0
-
3.3
-
ATP
-
pH 8.0, 25C
0.83
-
N-phosphotaurocyamine
-
pH 7.2, 25C
0.1
-
N-taurocyamine
-
pH 8.0, 25C
0.082
-
Taurocyamine
-
mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.14
-
Taurocyamine
-
mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.153
-
Taurocyamine
-
mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.184
-
Taurocyamine
-
mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.205
-
Taurocyamine
-
mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.217
-
Taurocyamine
-
mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.269
-
Taurocyamine
-
isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.278
-
Taurocyamine
-
mutant enzyme K95I, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.287
-
Taurocyamine
-
mutant enzyme K95R, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.313
-
Taurocyamine
-
mutant enzyme K95H, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.332
-
Taurocyamine
-
mutant enzyme T70A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.57
-
Taurocyamine
C7BCG0
-
0.603
-
Taurocyamine
-
mutant enzyme V71A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.718
-
Taurocyamine
-
mutant enzyme T68A, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.742
-
Taurocyamine
-
mutant enzyme K69R, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.813
-
Taurocyamine
-
mutant enzyme H67A, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.881
-
Taurocyamine
-
-
0.913
-
Taurocyamine
-
wild type enzyme, in 100 mM Tris-HCl, at pH 8.0 and 25C
0.969
-
Taurocyamine
-
isoform PK2, in 100 mM Tris-HCl, at pH 8.0 and 25C
1.228
-
Taurocyamine
-
mutant enzyme K69A, in 100 mM Tris-HCl, at pH 8.0 and 25C
1.868
-
Taurocyamine
-
mutant enzyme T70A, in 100 mM Tris-HCl, at pH 8.0 and 25C
2.091
-
Taurocyamine
-
mutant enzyme V71A, in 100 mM Tris-HCl, at pH 8.0 and 25C
2.12
-
Taurocyamine
Q4AEC7, Q4AEC8, -
-
4.01
-
Taurocyamine
-
-
13.28
-
Taurocyamine
-
mutant enzyme K95E, in 100 mM Tris-HCl, at pH 8.0 and 25C
33.44
-
Taurocyamine
C7BCG0
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.43
-
Taurocyamine
-
-
12.5
-
Taurocyamine
Q4AEC7, Q4AEC8, -
-
14.3
-
Taurocyamine
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
58.67
-
Taurocyamine
C7BCG0
-
16892
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.298
-
Q4AEC7, Q4AEC8, -
arginine
0.855
-
Q4AEC7, Q4AEC8, -
lombricine
1.32
-
-
glycocyamine
2.541
-
-
lombricine
3.25
-
Q4AEC7, Q4AEC8, -
lombricine
3.65
-
Q4AEC7, Q4AEC8, -
glycocyamine
4.04
-
Q4AEC7, Q4AEC8, -
taurocyamine
5.16
-
-
lombricine
10.4
-
Q4AEC7, Q4AEC8, -
taurocyamine
17.82
-
-
taurocyamine
28.71
-
-
taurocyamine
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
-
reaction with phosphotaurocyamine or hypophosphotaurocyamine
7.2
-
-
synthesis of ATP
8
-
-
synthesis of phosphotaurocyamine
8.5
-
-
reaction with hypotaurocyamine
9
-
-
reaction with taurocyamine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
45
-
20C: 70% of maximal activity, 45C: less than 45% of maximal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.62
-
-
calculated
7.9
-
C7BCG0
calculated from amino acid sequence
7.98
-
Q4AEC7, Q4AEC8, -
calculated
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 ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q4AEC7, Q4AEC8, -
a small part of the plume; a small part of the plume
Manually annotated by BRENDA team
Q4AEC7, Q4AEC8, -
;
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q4AEC7, Q4AEC8, -
-
Manually annotated by BRENDA team
Q4AEC5, Q4AEC6
annelid-specific enzyme
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40830
-
Q4AEC7, Q4AEC8, -
calculated from amino acid sequence
41350
-
-
calculated from amino acid sequence
46200
-
-
calculated from amino acid sequence
59000
-
-
gel filtration
61000
-
-
ultracentrifugation
80000
-
-
gel filtration
80000
-
P16641, -
-
80220
-
C7BCG0
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40000, isoform PK1, SDS-PAGE; x * 80000, isoform PK2, SDS-PAGE
additional information
-
SDS-PAGE reveals 3 protein bands: 11000 Da, 13000-14000 Da and 21000-22000 Da
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
P16641, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
stable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol does not stabilize
-
unstable to freezing
-
Unstable to lyophilization
-
structurally very unstable, gradual loss of enzyme activity even when it is stored on ice for several hours
Q4AEC7, Q4AEC8, -
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
recombinant protein is purified by affinity chromatography using amylose resin
-
amylose resin column chromatography, gel filtration
C7BCG0
recombinant protein is purified by affinity chromatography using amylose resin; recombinant protein is purified by affinity chromatography using amylose resin
Q4AEC7, Q4AEC8, -
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
P16641, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; expression in Escherichia coli TB1
-
the maltose binding protein-fused enzyme is expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli TB1 cells
C7BCG0
expression in Escherichia coli TB1; expression in Escherichia coli TB1
Q4AEC7, Q4AEC8, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
P16641, -
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