Literature summary extracted from
Pan, X.; Zhang, H.; Gao, Y.; Li, M.; Chang, W.
Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH. (2009), Biochem. Biophys. Res. Commun., 390, 597-602.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.6.5.5 |
crystal structures of zeta-crystallin-like quinone oxidoreductase and its complexes with NADPH determined at 2.4 and 2.01 A resolution |
Pseudomonas syringae |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.6.5.5 |
Pseudomonas syringae |
- |
pv. tomato DC3000 |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.6.5.5 |
2 1,4-benzoquinone + NADPH + H+ |
weak activity |
Pseudomonas syringae |
? + NADP+ |
- |
? |
|
1.6.5.5 |
2 9,10-phenanthrenequinone + NADPH + H+ |
very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. The zeta-crystallin-like quinone oxidoreductase catalyzes one-electron reduction of certain quinones to generate semiquinone |
Pseudomonas syringae |
2 9,10-phenanthrenesemiquinone + NADP+ |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.6.5.5 |
dimer |
PtoQOR forms as a homologous dimer, each monomer containing two domains |
Pseudomonas syringae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.6.5.5 |
PtoQOR |
- |
Pseudomonas syringae |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
1.6.5.5 |
25 |
- |
assay at |
Pseudomonas syringae |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
1.6.5.5 |
7.5 |
- |
assay |
Pseudomonas syringae |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.6.5.5 |
NADPH |
NADPH binding causes conformational changes in the structure of the enzyme |
Pseudomonas syringae |
|