Distribution of membrane-bound monoamine oxidase in bacteria

Abstract

The distribution of membrane-bound monoamine oxidase in 30 strains of various bacteria was studied. Monoamine oxidase was determined by using an ammonia-selective electrode; analyses were sensitive and easy to perform. The enzyme was found in some strains of the family Enterobacteriaceae, such as Klebsiella, Enterobacter, Escherichia, Salmonella, Serratia, and Proteus. Among strains of other families of bacteria tested, only Pseudomonas aeruginosa IFO 3901, Micrococcus luteus IFO 12708, and Brevibacterium ammoniagenes IAM 1641 had monoamine oxidase activity. In all of these bacteria except B. ammoniagenes, monoamine oxidase was induced by tyramine and was highly specific for tyramine, octopamine, dopamine, and norepinephrine. The enzyme in two strains oxidized histamine or benzylamine. Correlations between the distributions of membrane-bound monoamine oxidase and arylsulfatase synthesized in the presence of tyramine were discussed.

Genetic requirements for the expression of benzylamine dehydrogenase activity in Pseudomonas putida

“…Microbial degradation of aromatic amines proceeds via initial attack of either oxygen-dependent amine oxidases [1] or amine dehydrogenases employing intermediate electron acceptors [2^4]. An amine dehydrogenase enzyme of the latter class, oxidizing benzylamine to benzaldehyde ( Fig.…”

Genetic requirements for the expression of benzylamine dehydrogenase activity in Pseudomonas putida

“…Microbial degradation of aromatic amines proceeds via initial attack of either oxygen‐dependent amine oxidases [1] or amine dehydrogenases employing intermediate electron acceptors [2–4]. An amine dehydrogenase enzyme of the latter class, oxidizing benzylamine to benzaldehyde (Fig.…”

Two Different Quinohemoprotein Amine Dehydrogenases Initiate Anaerobic Degradation of Aromatic Amines in Aromatoleum aromaticum EbN1

“…In both cases, the amines are initially converted to aldehydes or ketones (from primary or secondary amines, respectively). Most of the known amine-oxidizing enzymes belong to the flavoenzymes and contain a flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) cofactor in their active sites, but some are known as quinoenzymes, containing several types of quinoid cofactors (2,4,5). The first characterized quinoenzymes were methanol dehydrogenase (6,7) and glucose oxidase, which contain the soluble cofactor pyrroloquinoline quinone (PQQ) in their active sites and oxidize alcohols or sugars rather than amines, but a growing number of additional amine-oxidizing quinoenzymes with covalently bound quinoid cofactors have been identified over the last 3 decades.…”