EC Number   |
General Information |
Reference |
|---|
    1.2.7.5 | evolution |
the aldehyde oxidoreductase belongs to the subfamily of tungsten-containing enzymes. AORAa appears to be a prototype of a distinct subfamily of bacterial AOR-like tungsten-enzymes, which differ from the previously known archaeal AORs mostly by their multi-subunit composition, their low sensitivity against oxygen, and the ability to use NAD+ as electron acceptor. Phylogenetic tree of the AOR enzyme family, overview |
-, 763075 |
| 1.2.7.5 | metabolism |
the enzyme is critical to ethanol formation |
740953 |
| 1.2.7.5 | more |
in contrast to previously known AORs, AORAa is a heterohexameric protein consisting of three different subunits, a large subunit containing the W-cofactor and an Fe-S cluster, a small subunit containing four Fe-S clusters, and a medium subunit containing an FAD cofactor |
-, 763075 |
| 1.2.7.5 | physiological function |
deletion of either subunit results in a distinct growth phenotype on both C5 and C6 sugars, with an increased lag phase, but higher cell densities. GOR functions in parallel with the conventional glyceraldehyde-3-phosphate dehydrogenase |
-, 763266 |
| 1.2.7.5 | physiological function |
the enzyme plays a role in peptide fermentation |
674251 |
| 1.2.7.5 | physiological function |
under constant control of gas pressure and pH at 0.1 MPa and 6.0, respectively, ethanol is formed during the exponential phase, closely accompanied by biomass production. Then, ethanol is oxidized to acetate via the aldehyde ferredoxin oxidoreductase pathway in Clostridium ljungdahlii. AOR2, as well as AdhE1, are responsible for ethanol oxidation during the stationary phase. Inactivation of Aor2 blocks the oxidation pathway, resulting in a high ethanol concentration in end products |
-, 762648 |
