2.7.3.4: taurocyamine kinase
This is an abbreviated version!
For detailed information about taurocyamine kinase, go to the full flat file.
Word Map on EC 2.7.3.4
-
2.7.3.4
-
creatine
-
glycocyamine
-
lombricine
-
annelid
-
polychaete
-
cdna-derived
-
arenicola
-
2.7.3.3
-
neanthes
-
paragonimus
-
phosphoarginine
-
westermani
-
drug development
-
pharmacology
- 2.7.3.4
- creatine
- glycocyamine
- lombricine
-
annelid
-
polychaete
-
cdna-derived
- arenicola
-
2.7.3.3
- neanthes
- paragonimus
- phosphoarginine
- westermani
- drug development
- pharmacology
Reaction
Synonyms
ATP:taurocyamine phosphotransferase, CsTK, guanidino kinase, hypotaurocyamine kinase, kinase (phosphorylating), taurocyamine, kinase, taurocyamine (phosphorylating), MiTK, More, phosphagen kinase, PK1, PK2, SmGK, taurocyamine kinase, taurocyamine phosphotransferase, TK, TPK
ECTree
2.7.3.4 taurocyamine kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.3.4 - taurocyamine kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
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
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
I60A
I63A
R58A
Y84A
Y84R
Y87A
Y87R
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
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
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
