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 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
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Taurine and hypotaurine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:taurocyamine N-phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-72-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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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
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
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-
-
?
ATP + glycocyamine
ADP + N-phosphoglycocyamine
show the reaction diagram
Q4AEC5, Q4AEC6
-
-
-
?
ATP + taurocyamine
ADP + N-phosphotaurocyamine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required, maximal activity at 10 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chloroacetophenone
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-
monoiodoacetate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2
ADP
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pH 7.2, 25C
0.98 - 3.3
ATP
0.83
N-phosphotaurocyamine
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pH 7.2, 25C
0.1
N-taurocyamine
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pH 8.0, 25C
0.082 - 33.44
Taurocyamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.43 - 14.3
Taurocyamine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58.67
Taurocyamine
Paragonimus westermani
C7BCG0
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1939
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.32
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glycocyamine
2.541
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lombricine
5.16
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lombricine
17.82
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taurocyamine
28.71
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taurocyamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
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reaction with phosphotaurocyamine or hypophosphotaurocyamine
7.2
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synthesis of ATP
8
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synthesis of phosphotaurocyamine
8.5
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reaction with hypotaurocyamine
9
-
reaction with taurocyamine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8
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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
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20C: 70% of maximal activity, 45C: less than 45% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.62
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calculated
7.9
calculated from amino acid sequence
8.55
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calculated
additional information
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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
a small part of the plume; a small part of the plume
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40830
calculated from amino acid sequence
41350
-
calculated from amino acid sequence
46200
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calculated from amino acid sequence
59000
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gel filtration
61000
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ultracentrifugation
80220
calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40000, isoform PK1, SDS-PAGE; x * 80000, isoform PK2, SDS-PAGE
additional information
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SDS-PAGE reveals 3 protein bands: 11000 Da, 13000-14000 Da and 21000-22000 Da
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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stable
642485
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol does not stabilize
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, no decrease of activity when the crude extract is kept frozen for several months
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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
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0C, 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
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli TB1
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expressed in Escherichia coli TB1 cells
expression in Escherichia coli TB1; expression in Escherichia coli TB1
the maltose binding protein-fused enzyme is expressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H67A
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the mutant shows a decreased Km value compared to the wild type enzyme
H67A/K95Y
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the mutant shows significantly decreased Km value compared to the wild type enzyme
K69A
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the mutant shows significantly increased Km value compared to the wild type enzyme
K69A/K95Y
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the mutant shows significantly decreased Km value compared to the wild type enzyme
K69R
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the mutant shows significantly decreased Km value compared to the wild type enzyme
K69R/K95Y
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the mutant shows significantly decreased Km value compared to the wild type enzyme
K95A
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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
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activity is largely lost in this mutant
K95H
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the mutant has a 3fold higher affinity for taurocyamine
K95I
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the mutant has a 3fold higher affinity for taurocyamine
K95R
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the mutant has a 3fold higher affinity for taurocyamine
K95Y
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an increase in substrate concentration causes a decrease in initial velocity of the reaction performed by this mutant (substrate inhibition)
T68A
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the mutant shows significantly decreased Km value compared to the wild type enzyme
T68AA/K95Y
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the mutant shows significantly decreased Km value compared to the wild type enzyme
T70A
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the mutant shows significantly increased Km value compared to the wild type enzyme
T70A/K95Y
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the mutant shows significantly decreased Km value compared to the wild type enzyme
V71A
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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
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the mutant shows significantly decreased Km value compared to the wild type enzyme
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