EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    1.1.5.8 | D-quinate + tetramethyl-p-phenylenediamine |
2,6-dichlorophenolindophenol can also act as electron acceptor |
Acinetobacter calcoaceticus |
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine |
- |
? |
| 1.1.5.8 | D-quinate + tetramethyl-p-phenylenediamine |
2,6-dichlorophenolindophenol can also act as electron acceptor |
Acinetobacter calcoaceticus LMD 79.41 |
3-dehydroquinate + reduced tetramethyl-p-phenylenediamine |
- |
? |
| 1.1.5.8 | more |
the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation |
Acinetobacter calcoaceticus |
? |
- |
? |
| 1.1.5.8 | more |
no oxidation of glucose, 3-dehydroquinate, 3-dehydroshikimate and myo-inositol |
Acinetobacter calcoaceticus |
? |
- |
? |
| 1.1.5.8 | more |
QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM |
Gluconobacter oxydans |
? |
- |
? |
| 1.1.5.8 | more |
QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm |
Gluconobacter oxydans |
? |
- |
- |
| 1.1.5.8 | more |
QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm |
Gluconobacter oxydans NBRC3293 |
? |
- |
- |
| 1.1.5.8 | more |
QDH activity is determined by the quinate-dependent ferricyanide reductase assay, QDH activity is also determined using phenazine methosulfate (PMS) and 2,6-dichlorophenolindophenol (DCIP) and measuring spectrophotometrically at 600 nm |
Gluconobacter oxydans NBRC3244 |
? |
- |
- |
| 1.1.5.8 | more |
QDH shows higher affinity to quinate, Km 1.0 mM, than to shikimate, Km 9.5 mM |
Gluconobacter oxydans IFO3244 |
? |
- |
? |
| 1.1.5.8 | more |
the enzyme is formed in presence or absence of quinate in the culture medium, although stronger induction is usually observed in the presence of quinate. The enzyme directly couples with the respiratory chain of the organisms, yielding bioenergy during substrate oxidation |
Acinetobacter calcoaceticus AC3 |
? |
- |
? |
