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Bioscience, Biotechnology, and Biochemistry Volume 69, 2005 - Issue 12
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Original Articles

Production of Completely Flavinylated Histamine Dehydrogenase, Unique Covalently Bound Flavin, and Iron–Sulfur Cluster-Containing Enzyme of Nocardioides simplex in Escherichia coli, and Its Properties

Nobutaka FUJIEDADivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
,
Noriaki TSUSEDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
,
Atsuko SATOHDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
,
Tokuji IKEDADivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
&
Kenji KANODivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
Pages 2459-2462 | Received 15 Jul 2005, Accepted 16 Sep 2005, Published online: 22 May 2014

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  • 2) Siddiqui, J. A., Shoeb, S. M., Takayama, S., Shimizu, E., and Yorifuji, T., Histamine dehydrogenase of Nocardioides simplex: a second bacterial enzyme for histamine degradation. J. Biochem. Mol. Biol. Biophys., 5, 37–43 (2001).
  • 3) McIntire, W. S., Wemmer, D. E., Chistoserdov, A., and Lidstrom, M. E., A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. Science, 252, 817–824 (1991).
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  • 5) Satoh, A., Kim, J. K., Miyahara, I., Devreese, B., Vandenberghe, I., Hacisalihoglu, A., Okajima, T., Kuroda, S., Adachi, O., Duine, J. A., Van Beeumen, J., Tanizawa, K., and Hirotsu, K., Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. J. Biol. Chem., 277, 2830–2834 (2002).
  • 6) Fujieda, N., Satoh, A., Tsuse, N., Kano, K., and Ikeda, T., 6-S-Cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme. Biochemistry, 43, 10800–10808 (2004).
  • 7) Steenkamp, D. J., and Mallinson, J., Trimethylamine dehydrogenase from a methylotrophic bacterium. I. Isolation and steady-state kinetics. Biochim. Biophys. Acta, 429, 705–719 (1976).
  • 8) Meiberg, J. B. M., and Harder, W., Aerobic and anaerobic metabolism of trimethylamine, dimethylamine and methylamine in Hyphomicrobium X. J. Gen. Microbiol., 115, 49–58 (1979).
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  • 10) Steenkamp, D. J., McIntire, W. S., and Kenney, W. C., Structure of the covalently bound coenzyme of trimethylamine dehydrogenase: evidence for a 6-substituted flavin. J. Biol. Chem., 253, 2818–2824 (1978).
  • 11) Limburg, J., Mure, M., and Klinman, J. P., Cloning and characterization of histamine dehydrogenase from Nocardioides simplex. Archives Biochem. Biophys., 436, 8–22 (2005).
  • 12) Takagi, K., and Shikata, S., Flow injection determination of histamine with a histamine dehydrogenase-based electrode. Anal. Chim. Acta, 505, 189–193 (2004).
  • 13) Hederstedt, L., Bergman, T., and Jijrnvall, H., Processing of Bacillus subtilis succinate dehydrogenase and cytochrome b-558 polypeptides: lack of covalently bound flavin in the Bacillus enzyme expressed in Escherichia coli. FEBS Lett., 213, 385–390 (1987).
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  • 15) Scrutton, N. S., Packman, L. C., Mathews, F. S., Rohlfs, R. J., and Hille, R., Assembly of redox centers in the trimethylamine dehydrogenase of bacterium W3A1: properties of the wild-type enzyme and a C30A mutant expressed from a cloned gene in Escherichia coli. J. Biol. Chem., 269, 13942–13950 (1994).
  • 16) Vanoni, M. A., Edmondson, D. E., Zanetti, G., and Curti, B., Characterization of the flavins and the iron–sulfur centers of glutamate synthase from Azospirillum brasilense by absorption, circular dichroism, and electron paramagnetic resonance spectroscopies. Biochemistry, 31, 4613–4623 (1992).
  • 17) Chen, J.-S., and Mortenson, L. E., Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron–sulfur protein samples containing dithionite. Anal. Biochem., 79, 157–165 (1977).
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