| Description | This entry represents the long-chain primary alcohol dehydrogenase AdhA (ADHA) from Thermoanaerobacter ethanolicus (formerly known as Clostridium thermohydrosulfuricum). This enzyme is an alcohol dehydrogenase active against primary long-chain alcohols that catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor [ ]. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. [, , ]. Members of this protein family are mainly found in bacteria and archaea. | Name | Long-chain primary alcohol dehydrogenase AdhA-like |
| Short Name | AdhA-like | Type | Family |
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