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Literature summary for 1.1.9.1 extracted from
- Deuterium isotope effect on enantioselectivity in the Comamonas testosteroni quinohemoprotein alcohol dehydrogenase-catalyzed kinetic resolution of rac-2,2-dimethyl-4-hydroxymethyl-1,3-dioxolane, solketal (2003), Biochim. Biophys. Acta, 1647, 297-302.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 2.2 | - |
ethanol | pH 7.5, 25°C | Comamonas testosteroni |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Comamonas testosteroni | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ethanol + ferricyanide | - |
Comamonas testosteroni | ethanal + ferrocyanide | - |
? | |
| rac-2,2-dimethyl-4-hydroxymethyl-1,3-dioxolane + ferricyanide | i.e. solketal. Enantiomeric ratio is 30 for solketal and 6 for rac-2,2-dimethyl-4-[1,1-2H]hydroxymethyl-1,3-[5,5,4-2H]dioxolane, d5-solketal. Isotopic substitution affects the relative kinetic weights of the initial hydron/deuteron transfer from substrate to cofactor and the subsequent proton/deuteron shift in the cofactor-product complex | Comamonas testosteroni | ? + ferrocyanide | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| quinohemoprotein alcohol dehydrogenase | - |
Comamonas testosteroni |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17.5 | - |
ethanol | pH 7.5, 25°C | Comamonas testosteroni | |
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