| Description | Butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway, in which it catalyses the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidised in the process. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Members in this family use divalent ions, preferentially iron or zinc [ ]. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3 [, ]. The active site of YqhD contains a zinc atom, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.This entry also includes Long-chain-alcohol dehydrogenase 2 from Geobacillus thermodenitrificans which is able to oxidise a broad range of alkyl alcohols from methanol to 1-triacontanol (C1 to C30), whose best substrate is 1-octanol. In contrast to other members of the family, it apparently does not use iron or other metals as cofactor [ ]. Aldehyde-alcohol dehydrogenase has both aldehyde and alcohol dehydrogenase activities. It can use acetaldehyde, butyraldehyde, butanol and ethanol. | Name | Butanol dehydrogenase-like |
| Short Name | BDH-like | Type | Family |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
