3.6.1.25: triphosphatase
This is an abbreviated version!
For detailed information about triphosphatase, go to the full flat file.
Word Map on EC 3.6.1.25
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3.6.1.25
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atpase
-
na+
-
ouabain
-
k+-adenosine
-
ca2+-adenosine
-
cardiac
-
sarcoplasmic
-
na+,k+-adenosine
-
k+-atpase
-
ca2+-atpase
-
myosin
-
parietal
-
guanylyltransferase
-
na+,k+-atpase
-
contractile
-
5'-nucleotidase
-
tripolyphosphate
-
ouabain-sensitive
-
omeprazole
-
ecto-adenosine
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inotropic
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antisecretory
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3.6.1.3
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digoxin
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diphosphatase
-
phospholamban
-
ecto-atpase
-
nak-atpase
-
lansoprazole
- 3.6.1.25
- atpase
- na+
- ouabain
-
k+-adenosine
-
ca2+-adenosine
- cardiac
-
sarcoplasmic
-
na+,k+-adenosine
-
k+-atpase
- ca2+-atpase
- myosin
-
parietal
-
guanylyltransferase
- na+,k+-atpase
-
contractile
- 5'-nucleotidase
- tripolyphosphate
-
ouabain-sensitive
- omeprazole
-
ecto-adenosine
-
inotropic
-
antisecretory
-
3.6.1.3
- digoxin
- diphosphatase
- phospholamban
- ecto-atpase
-
nak-atpase
- lansoprazole
Reaction
Synonyms
inorganic triphosphatase, triphosphate tunnel metalloenzyme, tripolyphosphatase, TTM
ECTree
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Engineering
Engineering on EC 3.6.1.25 - triphosphatase
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K52R
-
the His-tagged mutant loses 90-99% of its activity (catalytic efficiency is at least 1000times lower) compared to the wild type enzyme. Mn2+ does not induce a significant activation of this mutant
K85A
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the His-tagged mutant is about 10times less active than the wild type enzyme, but the optimal conditions for activity are essentially the same. The mutant is more strongly activated by Mn2+ than by Mg2+, and the inhibitory effects of Ca2+ and Zn2+ are less pronounced
K8A
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the His-tagged mutant remains highly active with tripolyphosphate as substrate and Mg2+ as activator, with a catalytic efficiency close to that of the recombinant wild type enzyme