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
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na+,k+-adenosine
-
k+-atpase
-
ca2+-atpase
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myosin
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parietal
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guanylyltransferase
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na+,k+-atpase
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contractile
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5'-nucleotidase
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tripolyphosphate
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ouabain-sensitive
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omeprazole
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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
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phospholamban
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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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Reference
Reference on EC 3.6.1.25 - triphosphatase
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Kulaev, I.S.; Konoshenko, G.I.; Umnov, A.M.
Localization of polyphosphatases hydrolyzing polyphosphates to orthophosphate in subcellular structures of Neurospora crassa
Biochemistry (Moscow)
37
190-194
1972
Neurospora crassa
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Kulalev, A.M.; Egorov, S.N.; Mansurova, S.E.; Kulaev, I.S.
A comparative characterization of the polyphosphatases of Neurospora crassa and some other organisms
Biochemistry (Moscow)
39
309-312
1974
Neurospora crassa
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Trilisenko, L.V.; Novotna, J.; Erban, V.; Behal, V.; Hostalek, Z.; Kulaev, I.S.
Subcellular localization of enzymes in Streptomyces aureofaciens and its alteration by benzyl thiocyanate
Folia Microbiol. (Praha)
32
402-410
1987
Kitasatospora aureofaciens
Yu, L.; Martins, A.; Deng, L.; Shuman, S.
Structure-function analysis of the triphosphatase component of vaccina virus mRNA capping enzyme
J. Virol.
71
9837-9843
1997
Vaccinia virus
Perez Mato, I.; Sanchez del Pino, M.M.; Chamberlin, M.E.; Mudd, S.H.; Mato, J.M.; Corrales, F.J.
Biochemical basis for the dominant inheritance of hypermethioninemia associated with the R264H mutation of the MAT1A gene. A monomeric methionine adenosyltransferase with tripolyphosphatase activity
J. Biol. Chem.
276
13803-13809
2001
Rattus norvegicus
Delvaux, D.; Murty, M.R.; Gabelica, V.; Lakaye, B.; Lunin, V.V.; Skarina, T.; Onopriyenko, O.; Kohn, G.; Wins, P.; De Pauw, E.; Bettendorff, L.
A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism
J. Biol. Chem.
286
34023-34035
2011
Nitrosomonas europaea
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