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Volumn 144, Issue 1, 2008, Pages 107-114

Purification and characterization of a copper-containing amine oxidase from Mycobacterium Sp. strain JC1 DSM 3803 grown on benzylamine

Author keywords

Amine oxidase; Benzylamine; Copper containing; Growth substrate; Semicarbazide sensitive

Indexed keywords

AMINE OXIDASE (COPPER CONTAINING); BENZYLAMINE; DIMER; HISTAMINE; SEMICARBAZIDE; TETRAMER; TYRAMINE;

EID: 46849114303     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvn047     Document Type: Article
Times cited : (11)

References (33)
  • 2
    • 0018118136 scopus 로고
    • A benzylamine oxidase distinct from monoamine oxidase B-widespread distribution in man and rat
    • Lewinsohn, R., Böhm, K., Glover, V., and Sandler, M. (1978) A benzylamine oxidase distinct from monoamine oxidase B-widespread distribution in man and rat. Biochem. Pharmacol. 27, 1857-1863
    • (1978) Biochem. Pharmacol , vol.27 , pp. 1857-1863
    • Lewinsohn, R.1    Böhm, K.2    Glover, V.3    Sandler, M.4
  • 3
    • 0031042325 scopus 로고    scopus 로고
    • Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca
    • Hacisalihoglu, A., Jongejan, J.A., and Duine, J.A. (1997) Distribution of amine oxidases and amine dehydrogenases in bacteria grown on primary amines and characterization of the amine oxidase from Klebsiella oxytoca. Microbiology 143, 505-512
    • (1997) Microbiology , vol.143 , pp. 505-512
    • Hacisalihoglu, A.1    Jongejan, J.A.2    Duine, J.A.3
  • 4
    • 0019394757 scopus 로고
    • Arthrobacter P1, a fast growing versatile methylotroph with amine oxidase as a key enzyme in the metabolism of methylated amines
    • Levering, P.R., van Dijken, J.P., Veenhius, M., and Harder, W. (1981) Arthrobacter P1, a fast growing versatile methylotroph with amine oxidase as a key enzyme in the metabolism of methylated amines. Arch. Microbiol. 129, 72-80
    • (1981) Arch. Microbiol , vol.129 , pp. 72-80
    • Levering, P.R.1    van Dijken, J.P.2    Veenhius, M.3    Harder, W.4
  • 5
    • 0016593557 scopus 로고
    • Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine
    • Buffoni, F. and Ignesti, G. (1975) Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine. J. Biochem. 145, 369-372
    • (1975) J. Biochem , vol.145 , pp. 369-372
    • Buffoni, F.1    Ignesti, G.2
  • 6
    • 0026060802 scopus 로고
    • Semicarbazide-sensitive amine oxidase activity (SSAO) of rat epididymal white adipose tissue
    • Raimondi, L., Pirisino, R., Ignesti, G., Capecchi, S., Banchelli, G., and Buffoni, F. (1991) Semicarbazide-sensitive amine oxidase activity (SSAO) of rat epididymal white adipose tissue. Biochem. Pharmacol. 41, 467-470
    • (1991) Biochem. Pharmacol , vol.41 , pp. 467-470
    • Raimondi, L.1    Pirisino, R.2    Ignesti, G.3    Capecchi, S.4    Banchelli, G.5    Buffoni, F.6
  • 7
    • 0018099544 scopus 로고
    • Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida
    • Durham, D.R. and Perry, J.J. (1978) Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida. J. Bacteriol. 134, 837-843
    • (1978) J. Bacteriol , vol.134 , pp. 837-843
    • Durham, D.R.1    Perry, J.J.2
  • 8
    • 0033602923 scopus 로고    scopus 로고
    • Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans
    • Takagi, K., Torimura, M., Kawaguchi, K., Kano, K., and Ikeda, T. (1999) Biochemical and electrochemical characterization of quinohemoprotein amine dehydrogenase from Paracoccus denitrificans. Biochemistry 38, 6935-6942
    • (1999) Biochemistry , vol.38 , pp. 6935-6942
    • Takagi, K.1    Torimura, M.2    Kawaguchi, K.3    Kano, K.4    Ikeda, T.5
  • 9
    • 0024617985 scopus 로고
    • Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803
    • Kim, K.S., Ro, Y.T., and Kim, Y.M. (1989) Purification and some properties of carbon monoxide dehydrogenase from Acinetobacter sp. strain JC1 DSM 3803. J. Bacteriol. 171, 958-964
    • (1989) J. Bacteriol , vol.171 , pp. 958-964
    • Kim, K.S.1    Ro, Y.T.2    Kim, Y.M.3
  • 10
    • 0012120561 scopus 로고    scopus 로고
    • Growth on methanol of a carboxydobacterium, Acinetobacter sp. Strain JC1 DSM 3803
    • Ro, Y.T., Seo, J.G., Lee, J.H., Kim, D.M., Chung, I.K., Kim, T.U., and Kim, Y.M. (1997) Growth on methanol of a carboxydobacterium, Acinetobacter sp. Strain JC1 DSM 3803. J. Microbiol. 35, 30-39
    • (1997) J. Microbiol , vol.35 , pp. 30-39
    • Ro, Y.T.1    Seo, J.G.2    Lee, J.H.3    Kim, D.M.4    Chung, I.K.5    Kim, T.U.6    Kim, Y.M.7
  • 11
    • 0346986108 scopus 로고    scopus 로고
    • Enzyme activities related to the methanol oxidation of Mycobacterium sp. strain JC1 DSM 3803
    • Ro, Y.T., Kim, E., and Kim, Y.M. (2000) Enzyme activities related to the methanol oxidation of Mycobacterium sp. strain JC1 DSM 3803. J. Microbiol. 38, 209-217
    • (2000) J. Microbiol , vol.38 , pp. 209-217
    • Ro, Y.T.1    Kim, E.2    Kim, Y.M.3
  • 13
    • 33745798660 scopus 로고    scopus 로고
    • Presence of an inducible semicarbazide-sensitive amine oxidase in Mycobacterium sp. Strain JC1 DSM 3803 grown on benzylamine
    • Ro, Y.T., Lee, H.I., and Kim, Y.M. (2006) Presence of an inducible semicarbazide-sensitive amine oxidase in Mycobacterium sp. Strain JC1 DSM 3803 grown on benzylamine. J. Microbiol. 44, 243-247
    • (2006) J. Microbiol , vol.44 , pp. 243-247
    • Ro, Y.T.1    Lee, H.I.2    Kim, Y.M.3
  • 14
    • 0019855290 scopus 로고
    • Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena
    • Kim, Y.M. and Hegeman, G.D. (1981) Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena. J. Bacteriol. 148, 904-911
    • (1981) J. Bacteriol , vol.148 , pp. 904-911
    • Kim, Y.M.1    Hegeman, G.D.2
  • 15
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • Newton-Vinson, P., Hubalek, F., and Edmondson, D.E. (2000) High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr. Purif. 20, 334-345
    • (2000) Protein Expr. Purif , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0036668044 scopus 로고    scopus 로고
    • Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibitor screening
    • Lee, M.H., Chuang, M.T, and Hou, W.C. (2002) Activity staining of plasma amine oxidase after polyacrylamide gel electrophoresis and its application to natural inhibitor screening. Electrophoresis 23, 2369-2372
    • (2002) Electrophoresis , vol.23 , pp. 2369-2372
    • Lee, M.H.1    Chuang, M.T.2    Hou, W.C.3
  • 18
    • 0025967971 scopus 로고
    • Specific detection of quinoproteins by redox-cycling staining
    • Paz, M.A., Flückiger, R., Boak, A., Kagan, H.M., and Gallop, P.M. (1991) Specific detection of quinoproteins by redox-cycling staining. J. Biol. Chem. 266, 689-692
    • (1991) J. Biol. Chem , vol.266 , pp. 689-692
    • Paz, M.A.1    Flückiger, R.2    Boak, A.3    Kagan, H.M.4    Gallop, P.M.5
  • 19
    • 0024741148 scopus 로고
    • Nitrogen metabolism in the facultative methylotroph Arthrobacter P1 grown with various amines or ammonia as nitrogen sources
    • De Boer, L., Brouwer, J.W., Van Hassel, C.W., Levering, P.R., and Dijkhuizen, L. (1989) Nitrogen metabolism in the facultative methylotroph Arthrobacter P1 grown with various amines or ammonia as nitrogen sources. Antonie Van Leeuwenhoek 56, 221-232
    • (1989) Antonie Van Leeuwenhoek , vol.56 , pp. 221-232
    • De Boer, L.1    Brouwer, J.W.2    Van Hassel, C.W.3    Levering, P.R.4    Dijkhuizen, L.5
  • 20
    • 0019630269 scopus 로고
    • Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source
    • Haywood, G.W. and Large, P.J. (1981) Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source. J. Biochem. 199, 187-201
    • (1981) J. Biochem , vol.199 , pp. 187-201
    • Haywood, G.W.1    Large, P.J.2
  • 21
    • 0014373548 scopus 로고
    • Amine oxidase. XII. The association and dissociation, and number of subunits of beef plasma amine oxidase
    • Achee, F.M., Chervenka, C.H., Smith, R.A., and Yasunobu, K.T. (1968) Amine oxidase. XII. The association and dissociation, and number of subunits of beef plasma amine oxidase. Biochemistry 7, 4329-4336
    • (1968) Biochemistry , vol.7 , pp. 4329-4336
    • Achee, F.M.1    Chervenka, C.H.2    Smith, R.A.3    Yasunobu, K.T.4
  • 22
    • 0016185034 scopus 로고
    • Analytical-band centrifugation of the active form of pig kidney diamine oxidase
    • Pionetti, J.M. (1974) Analytical-band centrifugation of the active form of pig kidney diamine oxidase. Biochem. Biophys. Res. Commun. 58, 495-498
    • (1974) Biochem. Biophys. Res. Commun , vol.58 , pp. 495-498
    • Pionetti, J.M.1
  • 23
    • 0032055852 scopus 로고    scopus 로고
    • Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase (SSAO) from bovine lung
    • Lizcano, J.M., Tipton, K.F., and Unzeta, M. (1998) Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase (SSAO) from bovine lung. J. Biochem. 331, 69-78
    • (1998) J. Biochem , vol.331 , pp. 69-78
    • Lizcano, J.M.1    Tipton, K.F.2    Unzeta, M.3
  • 24
    • 0025887806 scopus 로고
    • Structure-function studies of substrate oxidation by bovine serum amine oxidase: Relationship to cofactor structure and mechanism
    • Hartmann, C. and Klinman, J.P. (1991) Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism. Biochemistry 30, 4605-4611
    • (1991) Biochemistry , vol.30 , pp. 4605-4611
    • Hartmann, C.1    Klinman, J.P.2
  • 26
    • 0023869739 scopus 로고
    • Deamination of methylamine by semicarbazide-sensitive amine oxidase in human umbilical artery and rat aorta
    • Precious, E., Gunn, C.E., and Lyles, G.A. (1988) Deamination of methylamine by semicarbazide-sensitive amine oxidase in human umbilical artery and rat aorta. Biochem. Pharmacol. 37, 707-713
    • (1988) Biochem. Pharmacol , vol.37 , pp. 707-713
    • Precious, E.1    Gunn, C.E.2    Lyles, G.A.3
  • 27
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase
    • Janes, S.M., Mu, D., Wemmer, D., Smith, A.J., Kaur, S., Maltby, D., Burlingame, A.L., and Klinman, J.P. (1990) A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 248, 981-987
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.J.4    Kaur, S.5    Maltby, D.6    Burlingame, A.L.7    Klinman, J.P.8
  • 28
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
    • Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y., and Tanizawa, K. (1994) Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351, 360-364
    • (1994) FEBS Lett , vol.351 , pp. 360-364
    • Matsuzaki, R.1    Fukui, T.2    Sato, H.3    Ozaki, Y.4    Tanizawa, K.5
  • 29
    • 0014315754 scopus 로고
    • The effects of inhibitor mixtures and the specific effects of different anions on the oxidase activity of caeruloplasmin
    • Curzon, G. and Speyer, B.E. (1968) The effects of inhibitor mixtures and the specific effects of different anions on the oxidase activity of caeruloplasmin. J. Biochem. 109, 25-34
    • (1968) J. Biochem , vol.109 , pp. 25-34
    • Curzon, G.1    Speyer, B.E.2
  • 30
    • 0014883924 scopus 로고
    • Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity
    • Sunderman, F.W. Jr. and Nomoto, S. (1970) Measurement of human serum ceruloplasmin by its p-phenylenediamine oxidase activity. Clin. Chem. 16, 903-910
    • (1970) Clin. Chem , vol.16 , pp. 903-910
    • Sunderman Jr., F.W.1    Nomoto, S.2
  • 33
    • 0026722905 scopus 로고
    • Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases
    • Mu, D., Janes, S.M., Smith, A.J., Brown, D.E., Dooley, D.M., and Klinman, J.P. (1992) Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases. J. Biol. Chem. 267, 7979-7982
    • (1992) J. Biol. Chem , vol.267 , pp. 7979-7982
    • Mu, D.1    Janes, S.M.2    Smith, A.J.3    Brown, D.E.4    Dooley, D.M.5    Klinman, J.P.6


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