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Volume 146, Issue 4

Nicotinoprotein (NADH-containing) alcohol dehydrogenase from DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes

The EMBL accession number for the sequence reported in this paper is P81747.

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Abstract

Extracts from benzyl-alcohol-grown DSM 1069 showed NAD(P)-independent, ,-dimethyl-4-nitrosoaniline (NDMA)-dependent alcohol dehydrogenase activity. The enzyme exhibiting this activity was purified to homogeneity and characterized. It appears to be a typical nicotinoprotein as it contains tightly bound NADH acting as cofactor instead of coenzyme. Other characteristics indicate that it is highly similar to the known nicotinoprotein alcohol dehydrogenase (np-ADH) from : it is a homotetramer of 150 kDa; N-terminal amino acid sequencing (22 residues) showed that 77% of these amino acids are identical in the two enzymes; it has optimal activity at pH 70; it lacks NAD(P)H-dependent aldehyde reductase activity; it catalyses the oxidation of a broad range of (preferably) primary and secondary alcohols, either aliphatic or aromatic, and formaldehyde, with the concomitant reduction of the artificial electron acceptor NDMA. NDMA could be replaced by an aldehyde, but not formaldehyde, the substrate specificity of the enzyme for the aldehydes reflecting that for the corresponding alcohols. The latter also applied to the low aldehyde dismutase activity displayed by the enzyme. From this, together with the results of the induction studies, it is concluded that np-ADH functions as the main alcohol-oxidizing enzyme in the dissimilation of many, but not all, alcohols by and may also catalyse coenzyme-independent interconversion of alcohols and aldehydes under certain circumstances. It is anticipated that the enzyme may be of even wider significance since structural data indicate that np-ADH is also present in other (nocardioform) actinomycetes.

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Keyword(s): MNO, methanol:NDMA oxidoreductase , NDMA, N,N-dimethyl-4-nitrosoaniline , nicotinoprotein alcohol dehydrogenase , np-ADH, nicotinoprotein alcohol dehydrogenase and Rhodococcus erythropolis
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2000-04-01
2024-04-25
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Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Rhodococcus erythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydesThe EMBL accession number for the sequence reported in this paper is P81747.
Microbiology 146, 775 (2000); https://doi.org/10.1099/00221287-146-4-775
/content/journal/micro/10.1099/00221287-146-4-775
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