A novel flavin-containing monooxygenase from Methylophaga sp. strain SK1 and its indigo synthesis in Escherichia coli

Biochemical and Biophysical Research Communications

Volumn 306, Issue 4, 2003, Pages 930-936

  Choi, Hack Sun ^a   Kim, Jin Kwon ^a   Cho, Eun Hee ^a   Kim, Yong Chul ^b   Kim, Jae Il ^b   Kim, Si Wouk ^a  

^a Chosun University   (South Korea)

^b Gwangju Institute of Science and Technology (GIST)   (South Korea)

Author keywords

Flavin containing monooxygenase; Methylophaga sp. strain SK1; Microbial indigo synthesis

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; DIMER; DIMETHYLANILINE MONOOXYGENASE; FLAVINE ADENINE NUCLEOTIDE; PIGMENT; PROTEIN SUBUNIT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ABSORPTION SPECTROPHOTOMETRY; AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENETICS; BACTERIAL STRAIN; BIOCHEMISTRY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; EUKARYOTE; HUMAN; INDIGO; ISOELECTRIC POINT; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN MOTIF; SPECIES CULTIVATION; SYNTHESIS; YEAST;

ARABIDOPSIS; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; EUKARYOTA; INDIGOFERA; METHYLOPHAGA;

EID: 0038772084     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)01087-8     Document Type: Article

References (26)

1. Anthony C. The Biochemistry of methylotrophs. 1982;Academic press, New York.
2. Janvier M., Grimont P.A.D. The genus Methylophaga, a new line of descent within phylogenetic branch gamma of Proteobacteria. Res. Microbiol. 146:1995;543-550.
3. Zwart J.M.M., Nelisse P.N., Kuenen J.G. Isolation and characterization of Methylophaga sulfidovorans sp. nov.: an obligately methylotrophic, aerobic, dimethylsulfide oxidizing bacterium from a microbial mat. FEMS Microbiol. Ecol. 20:1996;261-270.
4. Ziegler D.M. Bioactivation of xenobiotics by flavin-containing monooxygenases. Adv. Exp. Med. Biol. 283:1991;41-50.
5. Goldberg J.B., Ohman D.E. Cloning and expression in Pseudomonas aeruginosa of a gene involved in the production of alginate. J. Bacteriol. 158:1984;1115-1121.
6. Whittenbury R.D.H. The methylotrophic bacteria. Starr M.P., Stolp H., Truper H.G., Balows A., Schlegel H.G. The Prokaryotes. 1981;894-902 Springer, Berlin.
7. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
8. Altschul S.F., Madden T.L., Schaffer A.A., Zhang J., Miller W., Lipman D.J. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 17:1997;3389-3402.
9. Karoly E.D., Rose R.L. Sequencing, expression, and characterization of cDNA expressed flavin-containing monooxygenase 2 from mouse. J. Biochem. Mol. Toxicol. 15:2001;300-308.
10. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
11. Zhang M., Robertus J.D. Molecular cloning and characterization of a full-length flavin-dependent monooxygenase from yeast. Arch. Biochem. Biophys. 403:2002;277-283.
12. Adachi J., Mori Y., Matsui S., Takigami H., Fujino J., Kitagawa H., Miller III C.A., Kato T., Saeki K., Matsuda T. Indirubin and indigo are potent aryl hydrocarbon receptor ligands present in human urine. J. Biol. Chem. 276:2001;31475-31478.
13. Fraaije M.W., Kamerbeek N.M., van Berkel W.J., Janssen D.B. Identification of a Baeyer-Villiger monooxygenase sequence motif. FEBS Lett. 518:2002;43-47.
14. Stehr M., Diekmann H., Smau L., Seth O., Ghisla S., Singh M., Macheroux P. A hydrophobic sequence motif common to N-hydroxylating enzymes. Trends Biochem. Sci. 23:1998;56-57.
15. Ziegler D.M. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab. Rev. 19:1988;1-32.
16. Agosin M., Ankley G.T. Conversion of N,N-dimethylanilineto to N,N-dimethylaniline-N-oxide N-oxide by a cytosolic flavin-containing enzyme from Trypanosoma cruzi. Drug Metab. Dispos. 15:1987;200-203.
17. Schlenk D. Occurrence of flavin-containing monooxygenases in non-mammalian eukaryotic organisms. Comp. Biochem. Physiol. C: Pharmacol. Toxicol. Endocrinol. 121:1998;185-195.
18. Kurelec B. Exclusive activation of aromatic amines in the marine mussel Mytilus edulis by FAD-containing monooxygenase. Biochem. Biophys. Res. Commun. 127:1985;773-778.
19. Zhao Y., Christensen S.K., Fankhauser C., Cashman J.R., Cohen J.D., Weigel D., Chory J. A role for flavin monooxygenase-like enzymes in auxin biosynthesis. Science. 291:2001;306-309.
20. Suh J.K., Poulsen L.L., Ziegler D.M., Robertus J.D. Redox regulation of yeast flavin-containing monooxygenase. Proc. Natl. Acad. Sci. USA. 96:1999;2687-2691.
21. Hodgson E., Levi P.E. The role of the flavin-containing monooxygenase (EC 1.14.13.8) in the metabolism and mode of action of agricultural chemicals. Xenobiotica. 22:1992;1175-1183.
22. Murdock D., Ensley B.D., Serdar C., Thalen M. Construction of metabolic operons catalyzing the de novo biosynthesis of indigo in Escherichia coli. Biotechnology. 11:1993;381-386.
23. Ensley B.D., Ratzkin B.J., Osslund T.D., Simon M.J., Wackett L.P., Gibson D.T. Expression of naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo. Science. 222:1983;167-169.
24. Hart S., Koch K.R., Woods D.R. Identification of indigo-related pigments produced by Escherichia coli containing a cloned Rhodococcus gene. J. Gen. Microbiol. 138:1992;211-216.
25. Drewlo S., Bramer C.O., Madkour M., Mayer F., Steinbuchel A. Cloning and expression of a Ralstonia eutropha HF39 gene mediating indigo formation in Escherichia coli. Appl. Environ. Microbiol. 67:2001;1964-1969.
26. Gillam E.M., Aguinaldo A.M., Notley L.M., Kim D., Mundkowski R.G., Volkov A.A., Arnold F.H., Soucek P., DeVoss J.J., Guengerich F.P. Formation of indigo by recombinant mammalian cytochrome P450. Biochem. Biophys. Res. Commun. 265:1999;469-472.