Growth stage-dependent expression of 6-hydroxy-d-nicotine oxidase of the nicotine regulon of Arthrobacter oxidans

Mauch, Ludwig; Krauß, Beate; Brandsch, Roderich

doi:10.1007/bf00447018

Cited by 6 publications

(2 citation statements)

References 18 publications

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“…This is the more surprising as both enzymes are expressed in the presence of DL-nicotine from the same plasmid within the same cell and share several enzymatic properties including similar binding characteristics for both enantiomeric substrates. However, the induction characteristics are different; nicotine dehydrogenase, 6-hydroxy-L-nicotine oxidase, and ketone dehydrogenase are induced synchronously during the logarithmic phase of growth of A. nicotinovorans, while 6-hydroxy-D-nicotine oxidase is formed mainly in stationary phase cells (Gloger and Decker 1969) and is under the control of a separate promotor (Mauch et al 1989). Similarly, the induction of 6-hydroxy-D-nicotine oxidase activity is insensitive to molybdate and tungstate, while the synthesis of 6-hydroxy-L-nicotine oxidase responds to the presence of these metals (GretherBeck et al 1994).…”

Section: Discussionmentioning

confidence: 99%

Horizontal Gene Transfer Involved in the Convergent Evolution of the Plasmid-Encoded Enantioselective 6-Hydroxynicotine Oxidases

Schenk

Decker

1999

J Mol Evol

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The D- and L-specific nicotine oxidases are flavoproteins involved in the oxidative degradation of nicotine by the Gram-positive soil bacterium Arthrobacter nicotinovorans. Their structural genes are located on a 160-kbp plasmid together with those of other nicotine-degrading enzymes. They are structurally unrelated at the DNA as well as at the protein level. Each of these oxidases possesses a high degree of substrate specificity; their catalytic stereoselectivity is absolute, although they are able to bind both enantiomeric substrates with a similar affinity. It appears that the existence of these enzymes is the result of convergent evolution. The amino acid sequence of 6-hydroxy-l-nicotine oxidase (EC 1.5.3.6) as derived from the respective structural gene shows considerable structural similarity with eukaryotic monoamine oxidases (EC 1.4.3.4) but not with monoamine oxidases from prokaryotic bacteria including those of the genus Arthrobacter. These similarities are not confined to the nucleotide-binding sites. A 100-amino acid stretch at the N-terminal regions of 6-hydroxy-l-nicotine oxidase and human monoamine oxidases A possess a 35% homology. Overall, 27.0, 26.9, and 25.8% of the amino acid positions of the monoamine oxidases of Aspergillus niger (N), humans (A), and rainbow trout (Salmo gairdneri) are identical to those of 6-hydroxy-l-nicotine oxidase (Smith-Waterman algorithm). In addition, the G+C content of the latter enzyme is in the range of that of eukaryotic monoamine oxidases and definitely lower than that of the A. nicotinovorans DNA and even that of the pAO1 DNA. The primary structure of 6-hydroxy-d-nicotine oxidase (EC 1.5.3.5) does not reveal its evolutionary history as easily. Significant similarities are found with a mitomycin radical oxidase from Streptomyces lavendulae (23.3%) and a "hypothetical protein" from Mycobacterium tuberculosis (26.0%). It is proposed that the plasmid-encoded gene of 6-hydroxy-l-nicotine oxidase evolved after horizontal transfer from an eukaryotic source.

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Section: Discussionmentioning

confidence: 99%

Horizontal Gene Transfer Involved in the Convergent Evolution of the Plasmid-Encoded Enantioselective 6-Hydroxynicotine Oxidases

Schenk

Decker

1999

J Mol Evol

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“…Moreover, further studies have shown that a riboflavin-126 dependent eo-regulation of the nicotine regulon genes occurs at the level of transcription (3,6). It is interesting that enzyme activity of 6-hydroxy-D-nicotine oxidase is induced in the stationary phase of cell growth, whereas all the other known enzymes in nicotine metabolism in A rthrobacter · oxidans are coordinately activated in the logarithmic phase (29). As previously stated, the ability of different strains of Arthrobacter oxidans to degrade nicotine seems to depend on the presence of the pA01 plasmid in bacteria.…”

Section: Induction and Regulation Of The Microbial Nicotine Metabolismmentioning

confidence: 94%

The Biological Degradation of Nicotine by Nicotinophilic Microorganisms

Eberhardt¹

1995

Beiträge Zur Tabakforschung International/Contributions to Tobacco Research

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Various microorganisms are capable of breaking down tobacco alkaloids by different biochemical processes and possess characteristic enzymatic systems for the catabolism of nicotine. Bacteria of the genus Pseudomonas and the fungus Cunninghamella echinulata degrade nicotine via N-methylmyosmine and pseudooxynicotine which is linked to the opening of the pyrrolidine ring (pyrrolidine pathway), whereas Arthrobacter oxidans hydroxylates the pyridine ring in the 6-position. 6-hydroxynicotine is pro-. duced as a primary product (pyridine pathway). Tobacco plants, and some fungi (e.g. Pellicularia filamentosa) degrade nicotine via demethylation to nornicotine (methyl pathway). As a result of the microbial degradation of nicotine and other tobacco alkaloids, carbon and nitrogen are made bioavailable. Following metabolic conversion to carboxylic acids, the reaction products are used by unicellular organisms as primary nutrients and a source of energy for the synthesis of new cell compounds. ZUSAMMENFASSUNGBestimmte Mikroorganismen kOnnen Tabakalkaloide iiber unterschiedliche biochemische Prozesse abbauen und besitzen charakteristische Enzymsysteme zur Katabolisierung von Nikotin. Bakterien der Gattung Pseudomonas und der Pilz Cunninghamella echinulata fiihren die Nikotinverstoffwechselung via N-Methylmyosmin und Pseudooxynikotin durch, wobei es zur 6ffnung des Pyrrolidin-Fiinfrings kommt. (Pyrrolidin-Stoffwechselweg). Im Gegensatz hierzu bevorzugt A rthrobacter oxidans eine Hydroxylierung in Position 6 des Pyridinringes. Es entsteht als primiires lntermediat 6-Hydroxynikotin (Pyridin-Stoffwechselweg). Die Tabakpflanzen und auch einige Pilze (z.B. Pellicularia filamentosa) verfiigen iiber die Fahigkeit, Nikotin unter Abspaltung der Methylgruppe in Nornikotin umzuwandeln (Methyl-Stoffwechselweg). Dutch den biologischen Abbau des Nikotins und weiterer Tabakalkaloide werden neue Kohlenstoff-und Stickstoffquellen von den Mikroorganismen erschlossen und nach der Metabolisierung zu Carbonsauren als energiereiche Substrate dem Primarstoffwechsel zur Synthese neuer Zellbestandteile und zur Energiegewinnung zur Verfiigung gestellt. RESUME ns existent des micro-organismes qui peuvent d&:omposer les alcaloi'des de tabac a !'aide de diffl:rents processus biochemiques et qui possMent des systemes enzymatiques caracreristiques pour rendre possible la catabolisation de la 119

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Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans 1 1Edited by J. Karn

Schenk

Hoelz

Krauβ

et al. 1998

Journal of Molecular Biology

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Growth stage-dependent expression of 6-hydroxy-d-nicotine oxidase of the nicotine regulon of Arthrobacter oxidans

Cited by 6 publications

References 18 publications

Horizontal Gene Transfer Involved in the Convergent Evolution of the Plasmid-Encoded Enantioselective 6-Hydroxynicotine Oxidases

Horizontal Gene Transfer Involved in the Convergent Evolution of the Plasmid-Encoded Enantioselective 6-Hydroxynicotine Oxidases

The Biological Degradation of Nicotine by Nicotinophilic Microorganisms

Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans 1 1Edited by J. Karn

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