1887

Abstract

The nucleotide sequence of the aromatic amine utilization () gene region from contained nine genes (, , , , and ) transcribed in the same direction. The and genes encode the periplasmic aromatic amine dehydrogenase (AADH) large and small subunit polypeptides, respectively, and were homologous to and , the genes for the large and small subunits of methylamine dehydrogenase (MADH). and are homologous to and and apparently carry out the same function of transport and folding of the small subunit polypeptide in the periplasm. No analogues of the , , , and genes responsible for biosynthesis of tryptophan tryptophylquinone (the prosthetic group of amine dehydrogenases) were found in the cluster. was predicted to encode a small periplasmic monohaem -type cytochrome. No biological function can be assigned to polypeptides encoded by , and and mutations in these genes appeared to be lethal. Mutants generated by insertions into were not able to use phenylethylamine, tyramine and tryptamine as a source of carbon and phenylethylamine, 3’-hydroxytyramine (dopamine) and tyramine as a source of nitrogen, indicating that AADH is the only enzyme involved in utilization of primary amines in . AADH genes are present in subsp. , but not in other β- and γ-proteobacteria. Phylogenetic analysis of amine dehydrogenases (MADH and AADH) indicated that AADH and MADH evolutionarily diverged before separation of proteobacteria into existing subclasses.

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2001-08-01
2020-01-19
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