EC Number   |
Substrates |
Organism  |
Products |
Reversibility |
|---|
    1.2.99.8 | acetaldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
acetate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | D-glyceraldehyde + H2O + acceptor |
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway |
Sulfolobus acidocaldarius |
D-glycerate + reduced acceptor |
- |
? |
| 1.2.99.8 | DL-glyceraldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
glycerate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | formaldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
formate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | glyceraldehyde-3-phosphate + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
3-phospho-D-glycerate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | isobutyraldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibits activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
isobutyrate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | more |
no activity with D-glucose. None of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol |
Sulfolobus acidocaldarius |
? |
- |
? |
| 1.2.99.8 | propionaldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius |
propionate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | acetaldehyde + 2,6-dichlorophenolindophenol + H2O |
none of the tested electron acceptors (Sulfolobus ferredoxin, cytochrome c, NAD+, NADP+, benzoquinones, naphthoquinones) supports aldehyde oxidation as efficiently as 2,6-dichlorophenolindophenol. At pH 7.5, the enzyme exhibited activity preferentially towards the aliphatic aldehydes formaldehyde, acetaldehyde and propionaldehyde. At pH 6.7, supposed to be close to the intracellular pH of Sulfolobus, glyceraldehyde is the predominant substrate |
Sulfolobus acidocaldarius DSM 639 |
acetate + reduced 2,6-dichlorophenolindophenol |
- |
? |
| 1.2.99.8 | D-glyceraldehyde + H2O + acceptor |
function as a glyceraldehyde oxidoreductase in the course of the nonphosphorylative Entner-Doudoroff pathway |
Sulfolobus acidocaldarius DSM 639 |
D-glycerate + reduced acceptor |
- |
? |
