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Volumn 119, Issue 3, 2005, Pages 260-271

Histamine dehydrogenase from Rhizobium sp.: Gene cloning, expression in Escherichia coli, characterization and application to histamine determination

Author keywords

6 S Cysteinyl FMN; Cloning; Enzymatic assay; Histamine; Histamine dehydrogenase; Substrate specificity

Indexed keywords

ABSORPTION; AMINES; AMINO ACIDS; COLORIMETRY; ESCHERICHIA COLI; REDOX REACTIONS;

EID: 24344454401     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.04.005     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 0003360433 scopus 로고
    • Histamine in seafood: Fluorometric method. Methods 35.1.32 and 977.13
    • AOAC P.A. Cunniff 16th ed. AOAC International Gaithersburg, MD
    • AOAC Histamine in seafood: fluorometric method. Methods 35.1.32 and 977.13 P.A. Cunniff Official Methods of Analysis of AOAC International 16th ed. 1995 AOAC International Gaithersburg, MD 16 17
    • (1995) Official Methods of Analysis of AOAC International , pp. 16-17
  • 2
    • 0036500999 scopus 로고    scopus 로고
    • Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenase
    • L. Bao, D. Sun, H. Tachikawa, and V.L. Davidson Improved sensitivity of a histamine sensor using an engineered methylamine dehydrogenase Anal. Chem. 74 2002 1144 1148
    • (2002) Anal. Chem. , vol.74 , pp. 1144-1148
    • Bao, L.1    Sun, D.2    Tachikawa, H.3    Davidson, V.L.4
  • 3
    • 0026739339 scopus 로고
    • Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase
    • M.J. Barber, P.N. Neame, L.W. Lim, S. White, and F.S. Mathews Correlation of X-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase J. Biol. Chem. 267 1992 6611 6619
    • (1992) J. Biol. Chem. , vol.267 , pp. 6611-6619
    • Barber, M.J.1    Neame, P.N.2    Lim, L.W.3    White, S.4    Mathews, F.S.5
  • 4
    • 0031056256 scopus 로고    scopus 로고
    • Selective modification of alkylammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-π bonding
    • J. Basran, M. Mewies, F.S. Mathews, and N.S. Scrutton Selective modification of alkylammonium ion specificity in trimethylamine dehydrogenase by the rational engineering of cation-π bonding Biochemistry 36 1997 1989 1998
    • (1997) Biochemistry , vol.36 , pp. 1989-1998
    • Basran, J.1    Mewies, M.2    Mathews, F.S.3    Scrutton, N.S.4
  • 5
    • 0035816680 scopus 로고    scopus 로고
    • Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase: Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes
    • J. Basran, M.J. Sutcliffe, and N.S. Scrutton Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase: implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes J. Biol. Chem. 276 2001 24581 24587
    • (2001) J. Biol. Chem. , vol.276 , pp. 24581-24587
    • Basran, J.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 6
    • 0035900665 scopus 로고    scopus 로고
    • Optimizing the Michaelis complex of trimethylamine dehydrogenase: Identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base
    • J. Basran, M.J. Sutcliffe, and N.S. Scrutton Optimizing the Michaelis complex of trimethylamine dehydrogenase: identification of interactions that perturb the ionization of substrate and facilitate catalysis with trimethylamine base J. Biol. Chem. 276 2001 42887 42892
    • (2001) J. Biol. Chem. , vol.276 , pp. 42887-42892
    • Basran, J.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 7
    • 0034868235 scopus 로고    scopus 로고
    • Trimethylamine and total volatile basic nitrogen determination by flow injection/gas diffusion in Mediterranean hake (Merluccius merluccius)
    • S. Baixas-Nogueras, S. Bover-Cid, M.C. Vidal-Carou, M.T. Veciana-Nogués, and A. Mariné-Font Trimethylamine and total volatile basic nitrogen determination by flow injection/gas diffusion in Mediterranean hake (Merluccius merluccius) J. Agric. Food Chem. 49 2001 1681 1686
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 1681-1686
    • Baixas-Nogueras, S.1    Bover-Cid, S.2    Vidal-Carou, M.C.3    Veciana-Nogués, M.T.4    Mariné-Font, A.5
  • 8
    • 0019964065 scopus 로고
    • The demonstration of histamine release in clinical conditions: A review of past and present assay procedures
    • M.A. Beaven, A. Robinson-White, N.B. Roderick, and G.L. Kauffman The demonstration of histamine release in clinical conditions: a review of past and present assay procedures Klin. Wochenschr. 60 1982 873 881
    • (1982) Klin. Wochenschr. , vol.60 , pp. 873-881
    • Beaven, M.A.1    Robinson-White, A.2    Roderick, N.B.3    Kauffman, G.L.4
  • 10
    • 0016312175 scopus 로고
    • Purification and properties of the trimethylamine dehydrogenase of bacterium 4B6
    • J. Colby, and L.J. Zatman Purification and properties of the trimethylamine dehydrogenase of bacterium 4B6 Biochem. J. 143 1974 555 567
    • (1974) Biochem. J. , vol.143 , pp. 555-567
    • Colby, J.1    Zatman, L.J.2
  • 11
    • 0014231042 scopus 로고
    • Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine
    • R.R. Eady, and P.J. Large Purification and properties of an amine dehydrogenase from Pseudomonas AM1 and its role in growth on methylamine Biochem. J. 106 1968 245 255
    • (1968) Biochem. J. , vol.106 , pp. 245-255
    • Eady, R.R.1    Large, P.J.2
  • 12
    • 0036942343 scopus 로고    scopus 로고
    • Human kidney diamine oxidase: Heterologous expression, purification, and characterization
    • B.O. Elmore, J.A. Bollinger, and D.M. Dooley Human kidney diamine oxidase: heterologous expression, purification, and characterization J. Biol. Inorg. Chem. 7 2002 565 579
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 565-579
    • Elmore, B.O.1    Bollinger, J.A.2    Dooley, D.M.3
  • 13
    • 4143133129 scopus 로고    scopus 로고
    • 6-S-Cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: Molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme
    • N. Fujieda, A. Satoh, N. Tsuse, K. Kano, and T. Ikeda 6-S-Cysteinyl flavin mononucleotide-containing histamine dehydrogenase from Nocardioides simplex: molecular cloning, sequencing, overexpression, and characterization of redox centers of enzyme Biochemistry 43 2004 10800 10808
    • (2004) Biochemistry , vol.43 , pp. 10800-10808
    • Fujieda, N.1    Satoh, A.2    Tsuse, N.3    Kano, K.4    Ikeda, T.5
  • 16
    • 0023217278 scopus 로고
    • Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
    • M. Husan, and V.L. Davidson Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans J. Bacteriol. 169 1987 1712 1717
    • (1987) J. Bacteriol. , vol.169 , pp. 1712-1717
    • Husan, M.1    Davidson, V.L.2
  • 17
    • 0037092976 scopus 로고    scopus 로고
    • Real-time monitoring of histamine released from rat basophilic leukemia (RBL-2H3) cells with a histamine microsensor using recombinant histamine oxidase
    • S. Iwaki, M. Ogasawara, R. Kurita, O. Niwa, K. Tanizawa, Y. Ohashi, and K. Maeyama Real-time monitoring of histamine released from rat basophilic leukemia (RBL-2H3) cells with a histamine microsensor using recombinant histamine oxidase Anal. Biochem. 304 2002 236 243
    • (2002) Anal. Biochem. , vol.304 , pp. 236-243
    • Iwaki, S.1    Ogasawara, M.2    Kurita, R.3    Niwa, O.4    Tanizawa, K.5    Ohashi, Y.6    Maeyama, K.7
  • 19
  • 21
    • 0018612053 scopus 로고
    • Hyphomicrobium X: Purification and some properties of a new enzyme that oxidizes secondary amines
    • J.B.M. Meinberg, and W. Harder Hyphomicrobium X: purification and some properties of a new enzyme that oxidizes secondary amines J. Genet. Microbiol. 115 1979 49 58
    • (1979) J. Genet. Microbiol. , vol.115 , pp. 49-58
    • Meinberg, J.B.M.1    Harder, W.2
  • 22
    • 0027965162 scopus 로고
    • Purification and characterization of diamine oxidase (histaminase) from rat small intestine
    • H. Mizuguchi, I. Imamura, M. Takemura, and H. Fukui Purification and characterization of diamine oxidase (histaminase) from rat small intestine J. Biochem. 116 1994 631 635
    • (1994) J. Biochem. , vol.116 , pp. 631-635
    • Mizuguchi, H.1    Imamura, I.2    Takemura, M.3    Fukui, H.4
  • 24
    • 0030606178 scopus 로고    scopus 로고
    • Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in Escherichia coli
    • I. Nishimura, K. Okada, and Y. Koyama Cloning and expression of pyranose oxidase cDNA from Coriolus versicolor in Escherichia coli J. Biotechnol. 52 1996 11 20
    • (1996) J. Biotechnol. , vol.52 , pp. 11-20
    • Nishimura, I.1    Okada, K.2    Koyama, Y.3
  • 25
    • 0023062476 scopus 로고
    • Aromatic amine dehydrogenase from Alcaligenes faecalis
    • M. Nozaki Aromatic amine dehydrogenase from Alcaligenes faecalis Meth. Enzymol. 142 1987 650 655
    • (1987) Meth. Enzymol. , vol.142 , pp. 650-655
    • Nozaki, M.1
  • 26
    • 0029042983 scopus 로고
    • The flavinylation reaction of trimethylamine dehydrogenase
    • L.C. Packman, M. Mewies, and N.S. Scrutton The flavinylation reaction of trimethylamine dehydrogenase J. Biol. Chem. 270 1995 13186 13191
    • (1995) J. Biol. Chem. , vol.270 , pp. 13186-13191
    • Packman, L.C.1    Mewies, M.2    Scrutton, N.S.3
  • 28
    • 0030957182 scopus 로고    scopus 로고
    • Purification and characterization of diamine oxidase from porcine kidney and intestine
    • H.G. Schwelberger, and E. Bodner Purification and characterization of diamine oxidase from porcine kidney and intestine Biochim. Biophys. Acta 1340 1997 152 164
    • (1997) Biochim. Biophys. Acta , vol.1340 , pp. 152-164
    • Schwelberger, H.G.1    Bodner, E.2
  • 30
    • 0034754969 scopus 로고    scopus 로고
    • Flow-through chemiluminescence sensor using immobilized histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007 and peroxidase for selective determination of histamine
    • Y. Sekiguchi, A. Nishikawa, H. Makita, A. Yamamura, K. Matsumoto, and N. Kiba Flow-through chemiluminescence sensor using immobilized histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007 and peroxidase for selective determination of histamine Anal. Sci. 17 2001 1161 1164
    • (2001) Anal. Sci. , vol.17 , pp. 1161-1164
    • Sekiguchi, Y.1    Nishikawa, A.2    Makita, H.3    Yamamura, A.4    Matsumoto, K.5    Kiba, N.6
  • 31
    • 1542357594 scopus 로고    scopus 로고
    • A thermostable histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007
    • Y. Sekiguchi, H. Makita, A. Yamamura, and K. Matsumoto A thermostable histamine oxidase from Arthrobacter crystallopoietes KAIT-B-007 J. Biosci. Bioeng. 97 2004 104 110
    • (2004) J. Biosci. Bioeng. , vol.97 , pp. 104-110
    • Sekiguchi, Y.1    Makita, H.2    Yamamura, A.3    Matsumoto, K.4
  • 33
    • 0034663742 scopus 로고    scopus 로고
    • Purification and characterization of histamine dehydrogenase from Nocardioides simplex IFO 12069
    • J.A. Siddiqui, S.M. Shoeb, S. Takayama, E. Shimizu, and T. Yorifuji Purification and characterization of histamine dehydrogenase from Nocardioides simplex IFO 12069 FEMS Microbiol. Lett. 189 2000 183 187
    • (2000) FEMS Microbiol. Lett. , vol.189 , pp. 183-187
    • Siddiqui, J.A.1    Shoeb, S.M.2    Takayama, S.3    Shimizu, E.4    Yorifuji, T.5
  • 35
    • 84964316661 scopus 로고
    • Biogenic amines in cheese and other fermented foods: A review
    • J.E. Stratton, R.W. Hutkins, and S.L. Taylor Biogenic amines in cheese and other fermented foods: a review J. Food Protect. 54 1991 460 470
    • (1991) J. Food Protect. , vol.54 , pp. 460-470
    • Stratton, J.E.1    Hutkins, R.W.2    Taylor, S.L.3
  • 36
    • 1042275672 scopus 로고    scopus 로고
    • Flow injection determination of histamine with a histamine dehydrogenase-based electrode
    • K. Takagi, and S. Shikata Flow injection determination of histamine with a histamine dehydrogenase-based electrode Anal. Chim. Acta 505 2004 189 193
    • (2004) Anal. Chim. Acta , vol.505 , pp. 189-193
    • Takagi, K.1    Shikata, S.2
  • 37
    • 0022996367 scopus 로고
    • Histamine food poisoning: Toxicology and clinical aspects
    • S.L. Taylor Histamine food poisoning: toxicology and clinical aspects Crit. Rev. Toxicol. 17 1986 91 128
    • (1986) Crit. Rev. Toxicol. , vol.17 , pp. 91-128
    • Taylor, S.L.1
  • 38
    • 0024829836 scopus 로고
    • Histamine poisoning (scombroid fish poisoning): An allergy-like intoxication
    • S.L. Taylor, J.E. Stratton, and J.A. Nordlee Histamine poisoning (scombroid fish poisoning): an allergy-like intoxication J. Toxicol. Clin. Toxicol. 27 1989 225 240
    • (1989) J. Toxicol. Clin. Toxicol. , vol.27 , pp. 225-240
    • Taylor, S.L.1    Stratton, J.E.2    Nordlee, J.A.3
  • 39
    • 84948637810 scopus 로고
    • Amine oxidase of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger
    • H. Yamada, O. Adachi, and K. Ogata Amine oxidase of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger Agric. Biol. Chem. 29 1965 864 869
    • (1965) Agric. Biol. Chem. , vol.29 , pp. 864-869
    • Yamada, H.1    Adachi, O.2    Ogata, K.3
  • 40
    • 0035305278 scopus 로고    scopus 로고
    • Bioelectrocatalytic detection of histamine using quinohemoprotein amine dehydrogenase and the native electron acceptor cytochrome c-550
    • K. Yamamoto, K. Takagi, K. Kano, and T. Ikeda Bioelectrocatalytic detection of histamine using quinohemoprotein amine dehydrogenase and the native electron acceptor cytochrome c-550 Electroanalysis 13 2001 375 379
    • (2001) Electroanalysis , vol.13 , pp. 375-379
    • Yamamoto, K.1    Takagi, K.2    Kano, K.3    Ikeda, T.4
  • 41
    • 85007978671 scopus 로고
    • Simultaneous determination of polyamine in red meat fishes by high performance liquid chromatography and evaluation of freshness
    • H. Yamanaka, and M. Matsumoto Simultaneous determination of polyamine in red meat fishes by high performance liquid chromatography and evaluation of freshness J. Food Hyg. Soc. Jpn. 30 1989 396 400
    • (1989) J. Food Hyg. Soc. Jpn. , vol.30 , pp. 396-400
    • Yamanaka, H.1    Matsumoto, M.2
  • 42
    • 0029166692 scopus 로고
    • The primary structure of Hyphomicrobium X dimethylamine dehydrogenase
    • C.-C. Yang, L.C. Packman, and N.S. Scrutton The primary structure of Hyphomicrobium X dimethylamine dehydrogenase Eur. J. Biochem. 232 1995 264 271
    • (1995) Eur. J. Biochem. , vol.232 , pp. 264-271
    • Yang, C.-C.1    Packman, L.C.2    Scrutton, N.S.3


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