Literature summary extracted from
McGee, D.J.; Kumar, S.; Viator, R.J.; Bolland, J.R.; Ruiz, J.; Spadafora, D.; Testerman, T.L.; Kelly, D.J.; Pannell, L.K.; Windle, H.J.
Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses (2006), J. Biol. Chem., 281, 3290-3296.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.5.3.1 |
Trx1 |
thioredoxin Trx1, stimulation by acting as a chaperone |
Helicobacter pylori |
|
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
3.5.3.1 |
diethylene triamine-nitric oxide |
50% inhibition at 2 mM |
Helicobacter pylori |
|
3.5.3.1 |
hydrogen peroxide |
50% inhibition at 0.003 mM |
Helicobacter pylori |
|
3.5.3.1 |
S-nitrosoglutathione |
50% inhibition at 0.050 mM |
Helicobacter pylori |
|
3.5.3.1 |
sodium nitroprusside |
50% inhibition at 0.005 mM |
Helicobacter pylori |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.5.3.1 |
Helicobacter pylori |
- |
- |
- |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
3.5.3.1 |
renaturation of heat- or urea-denatured enzyme by chaperone thioredoxin Trx1 from Helicobacter pylori extracts |
Helicobacter pylori |