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(R)-6-Hydroxynicotine oxidase

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Springer Handbook of Enzymes

Part of the book series: Springer Handbook of Enzymes ((HDBKENZYMES,volume 23))

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References

  1. Schenk, S.; Decker, K.: Horizontal gene transfer involved in the convergent evolution of the plasmid-encoded enantioselective 6-hydroxynicotine oxidases. J. Mol. Evol., 48, 178–186. (1999)

    Article  PubMed  CAS  Google Scholar 

  2. Stoltz, M.; Brandsch, R.: The conformational change induced by FAD in covalently flavinylated 6-hydroxy-D-nicotine oxidase does not require (8α)FAD(N3)histidyl bond formation. J. Biochem., 123, 445–449 (1998)

    PubMed  CAS  Google Scholar 

  3. Schenk, S.; Hoelz, A.; Krauss, B.; Decker, K.: Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans. J. Mol. Biol., 284, 1323–1339 (1998)

    Article  PubMed  CAS  Google Scholar 

  4. Stoltz, M.; Rassow, J.; Bueckmann, A.F.; Brandsch, R.: Covalent attachment of FAD derivatives to a fusion protein consisting of 6-hydroxy-D-nicotine oxidase and a mitochondrial presequence. Folding, enzyme activity, and import of the modified protein into yeast mitochondria. J. Biol. Chem., 271, 25208–25212 (1996)

    Article  PubMed  CAS  Google Scholar 

  5. Stoltz, M.; Henninger, H.P.; Brandsch, R.: The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD. FEBS Lett., 386, 194–196 (1996)

    Article  PubMed  CAS  Google Scholar 

  6. Stoltz, M.; Rysavy, P.; Kalousek, F.; Brandsch, R.: Folding, flavinylation, and mitochondrial import of 6-hydroxy-D-nicotine oxidase fused to the presequence of rat dimethylglycine dehydrogenase. J. Biol. Chem., 270, 8016–8022 (1995)

    Article  PubMed  CAS  Google Scholar 

  7. Grether-Beck, S.; Igloi, G.L.; Pust, S.; Schilz, E.; Decker, K.; Brandsch, R.: Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol., 13, 929–936 (1994)

    Article  PubMed  CAS  Google Scholar 

  8. Brandsch, R.; Bichler, V.; Mauch, L.; Decker, K.: Cysteine to serine replacements in 6-hydroxy-D-nicotine oxidase. Consequences for enzyme activity, cofactor incorporation, and formation of high molecular weight protein complexes with molecular chaperones (GroEL). J. Biol. Chem., 268, 12724–12729 (1993)

    PubMed  CAS  Google Scholar 

  9. Brandsch, R.; Bichler, V.; Schmidt, M.; Buchner, J.: GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase. J. Biol. Chem., 267, 20844–20849 (1992)

    PubMed  CAS  Google Scholar 

  10. Brandsch, R.; Bichler, V.: Autoflavinylation of apo6-hydroxy-D-nicotine oxidase. J. Biol. Chem., 266, 19056–19062 (1991)

    PubMed  CAS  Google Scholar 

  11. Mauch, L.; Bichler, V.; Brandsch, R.: Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase. J. Biol. Chem., 265, 12761–12762 (1990)

    PubMed  CAS  Google Scholar 

  12. Brandsch, R.; Bichler, V.; Krauss, B.: Binding of FAD to 6-hydroxy-D-nicotine oxidase apoenzyme prevents degradation of the holoenzyme. Biochem. J., 258, 187–192 (1989)

    PubMed  CAS  Google Scholar 

  13. Brandsch, R.; Bichler, V.: Covalent cofactor binding to flavoenzymes requires specific effectors. Eur. J. Biochem., 182, 125–128 (1989)

    Article  PubMed  CAS  Google Scholar 

  14. Brandsch, R.; Hinkkanen, A.E.; Mauch, L.; Nagursky, H.; Decker, K.: 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-l-nicotine oxidase. Eur. J. Biochem., 167, 315–320 (1987)

    Article  PubMed  CAS  Google Scholar 

  15. Brandsch, R.; Faller, W.; Schneider, K.: Plasmid pAO1 of Arthrobacter oxidans encodes 6-hydroxy-D-nicotine oxidase: cloning and expression of the gene in Escherichia coli. Mol. Gen. Genet., 202, 96–101 (1986)

    Article  PubMed  CAS  Google Scholar 

  16. Brandsch, R.; Bichler, V.: In vivo and in vitro expression of the 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans, cloned into Escherichia coli, as an enzymatically active, covalently flavinylated polypeptide. FEBS Lett., 192, 204–208 (1985)

    Article  PubMed  CAS  Google Scholar 

  17. Swafford, J.R.; Reeves, H.C.; Brandsch, R.: Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry. J. Bacteriol., 163, 792–795 (1985)

    PubMed  CAS  Google Scholar 

  18. Hinkkanen, A.; Lilius, E.M.; Nowack, J.; Maas, R.; Decker, K.: Purification of the flavoproteins 6-hydroxy-D-and 6-hydroxy-l-nicotine oxidase using hydrophobic affinity chromatography. Hoppe-Seyler’s Z. Physiol. Chem., 364, 801–806 (1983)

    PubMed  CAS  Google Scholar 

  19. Decker, K.: Structure and synthesis of a flavoprotein with covalently bound FAD. Trends Biochem. Sci., 1, 184–185 (1976)

    CAS  Google Scholar 

  20. Bruhmuller, M.; Möhler, H.; Decker, K.: Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Purification and properties of D-6-hydroxynicotine oxidase. Eur. J. Biochem., 29, 143–151 (1972)

    Article  PubMed  CAS  Google Scholar 

  21. Möhler, H.; Bruhmuller, M.; Decker, K.: Covalently bound flavin in D-6-hydroxynicotine oxidase from Arthrobacter oxidans. Identification of the 8-(N-3-histidyl)-riboflavin-linkage between FAD and apoenzyme. Eur. J. Biochem., 29, 152–155 (1972)

    Article  PubMed  Google Scholar 

  22. Decker, K.; Dai, V.D.: Mechanism and specifcity of l-and D-6-hydroxynicotine oxidase. Eur. J. Biochem., 3, 132–138 (1967)

    Article  PubMed  CAS  Google Scholar 

  23. Decker, K.; Bleeg, H.: Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans. Biochim. Biophys. Acta, 105, 313–324 (1965)

    PubMed  CAS  Google Scholar 

  24. Dai, V.D.; Decker, K.; Sund, H.: Purification and properties of l-6-hydroxynicotine oxidase. Eur. J. Biochem., 4, 95–102 (1968)

    Article  PubMed  CAS  Google Scholar 

  25. Decker, K.; Dai, V.D.; Möhler, H.; Bruhmuller, M.: D-and l-6-hydroxynicotine oxidase, enantioenzymes of Arthrobacter oxidans. Z. Naturforsch. B, 27, 1072–1073 (1972)

    PubMed  CAS  Google Scholar 

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  1. Institute for Biochemistry, University to Cologne, Zülpicher Strasse 47, 50674, Cologne, Germany

    Dietmar Schomburg  & Ida Schomburg  & 

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(2005). (R)-6-Hydroxynicotine oxidase. In: Schomburg, D., Schomburg, I. (eds) Springer Handbook of Enzymes. Springer Handbook of Enzymes, vol 23. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-37648-8_40

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