메뉴 건너뛰기




Volumn 46, Issue 6, 2010, Pages 487-493

Investigating antimicrobial activity in Rheinheimera sp. due to hydrogen peroxide generated by l-lysine oxidase activity

Author keywords

Antibiogram assay; Antimicrobial activity; Hydrogen peroxide; L Lysine oxidase; Phylogenetic analyses; Rheinheimera

Indexed keywords

16S RRNA GENE SEQUENCE; AMINO ACID FRAGMENTS; ANTI-MICROBIAL ACTIVITY; ANTI-MICROBIAL EFFECTS; ANTIBACTERIAL PROTEINS; BACTERIAL STRAINS; BROAD SPECTRUM; CULTURE MEDIA; ENZYMATIC ACTIVITIES; FRESHWATER BACTERIA; GRAM-NEGATIVE BACTERIA; ISO-ELECTRIC POINTS; L-LYSINE; LIQUID CHROMATOGRAPHY-TANDEM MASS SPECTROMETRY; MARINE BACTERIUM; MARINOMONAS; MONOMERIC PROTEINS; OXIDASE ACTIVITY; PHYLOGENETIC ANALYSES; PHYLOGENETIC ANALYSIS; PSEUDOALTEROMONAS;

EID: 77950341454     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2010.01.006     Document Type: Article
Times cited : (36)

References (64)
  • 1
    • 7644238048 scopus 로고    scopus 로고
    • Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes
    • Levy O. Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes. J Leukoc Biol 2004, 76:909-925.
    • (2004) J Leukoc Biol , vol.76 , pp. 909-925
    • Levy, O.1
  • 4
    • 0032006153 scopus 로고    scopus 로고
    • Instruments of microbial warfare: bacteriocin synthesis, toxicity and immunity
    • Baba T., Schneewind O. Instruments of microbial warfare: bacteriocin synthesis, toxicity and immunity. Trends Microbiol 1998, 6:66-71.
    • (1998) Trends Microbiol , vol.6 , pp. 66-71
    • Baba, T.1    Schneewind, O.2
  • 5
    • 50849108830 scopus 로고    scopus 로고
    • Lysostaphin: an antistaphylococcal agent
    • Kumar J.K. Lysostaphin: an antistaphylococcal agent. Appl Microbiol Biotechnol 2008, 80:555-561.
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 555-561
    • Kumar, J.K.1
  • 6
    • 0025083166 scopus 로고
    • Antagonistic activities of lactic acid bacteria in food and feed fermentations
    • Lindgren S.E., Dobrogosz W.J. Antagonistic activities of lactic acid bacteria in food and feed fermentations. FEMS Microbiol Rev 1990, 87:149-163.
    • (1990) FEMS Microbiol Rev , vol.87 , pp. 149-163
    • Lindgren, S.E.1    Dobrogosz, W.J.2
  • 7
    • 0033945724 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract
    • Pericone C.D., Overweg K., Hermans P.W., Weiser J.N. Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect Immun 2000, 68:3990-3997.
    • (2000) Infect Immun , vol.68 , pp. 3990-3997
    • Pericone, C.D.1    Overweg, K.2    Hermans, P.W.3    Weiser, J.N.4
  • 8
    • 27144509129 scopus 로고    scopus 로고
    • Competition and coexistence between Streptococcus mutans and Streptococcus sanguinis in the dental biofilm
    • Kreth J., Merritt J., Shi W., Qi F. Competition and coexistence between Streptococcus mutans and Streptococcus sanguinis in the dental biofilm. J Bacteriol 2005, 187:7193-7203.
    • (2005) J Bacteriol , vol.187 , pp. 7193-7203
    • Kreth, J.1    Merritt, J.2    Shi, W.3    Qi, F.4
  • 9
    • 29544451026 scopus 로고
    • Studies on the mechanism of action of l-amino acid oxidase
    • Wellner D., Meister A. Studies on the mechanism of action of l-amino acid oxidase. J Biol Chem 1961, 236:2357-2364.
    • (1961) J Biol Chem , vol.236 , pp. 2357-2364
    • Wellner, D.1    Meister, A.2
  • 10
    • 0025784241 scopus 로고
    • Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis venom
    • Stiles B.G., Sexton F.W., Weinstein S.A. Antibacterial effects of different snake venoms: purification and characterization of antibacterial proteins from Pseudechis australis venom. Toxicon 1991, 29:1129-1141.
    • (1991) Toxicon , vol.29 , pp. 1129-1141
    • Stiles, B.G.1    Sexton, F.W.2    Weinstein, S.A.3
  • 11
    • 0036234815 scopus 로고    scopus 로고
    • Snake venom l-amino acid oxidases
    • Du X.Y., Clemetson K.J. Snake venom l-amino acid oxidases. Toxicon 2002, 40:659-665.
    • (2002) Toxicon , vol.40 , pp. 659-665
    • Du, X.Y.1    Clemetson, K.J.2
  • 12
    • 26844491279 scopus 로고    scopus 로고
    • Cloning, characterization, and expression of escaping, a broadly antimicrobial FAD-containing l-amino acid oxidase from ink of the sea hare Aplysia californica
    • Yang H., Johnson P.M., Ko K.C., Kamio M., Germann M.W., Derby C.D., et al. Cloning, characterization, and expression of escaping, a broadly antimicrobial FAD-containing l-amino acid oxidase from ink of the sea hare Aplysia californica. J Exp Biol 2005, 208:3609-3622.
    • (2005) J Exp Biol , vol.208 , pp. 3609-3622
    • Yang, H.1    Johnson, P.M.2    Ko, K.C.3    Kamio, M.4    Germann, M.W.5    Derby, C.D.6
  • 13
    • 29544443905 scopus 로고    scopus 로고
    • Drug discovery and sea hares: bigger is better
    • Barsby T. Drug discovery and sea hares: bigger is better. Trends Biotechnol 2006, 24:1-3.
    • (2006) Trends Biotechnol , vol.24 , pp. 1-3
    • Barsby, T.1
  • 14
    • 57049171545 scopus 로고    scopus 로고
    • Identification of potent bactericidal compounds produced by escaping, an l-amino acid oxidase in the ink of the sea hare Aplysia californica
    • Ko K.C., Wang B., Tai P.C., Derby C.D. Identification of potent bactericidal compounds produced by escaping, an l-amino acid oxidase in the ink of the sea hare Aplysia californica. Antimicrob Agents Chemother 2008, 52:4455-4462.
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 4455-4462
    • Ko, K.C.1    Wang, B.2    Tai, P.C.3    Derby, C.D.4
  • 16
    • 0036955280 scopus 로고    scopus 로고
    • L-Lysine α-oxidase: physicochemical and biological properties
    • Lukasheva E.V., Berezov T.T. l-Lysine α-oxidase: physicochemical and biological properties. Biochemistry 2002, 67:1394-1402.
    • (2002) Biochemistry , vol.67 , pp. 1394-1402
    • Lukasheva, E.V.1    Berezov, T.T.2
  • 17
    • 0027988115 scopus 로고
    • Characterization of an antibiotic produced by Alteromonas luteoviolacea Gauthier 1982, 85 isolated from Kinko Bay, Japan
    • McCarthy S.A., Johnson R.M., Kakimoto D. Characterization of an antibiotic produced by Alteromonas luteoviolacea Gauthier 1982, 85 isolated from Kinko Bay, Japan. J Appl Bacteriol 1994, 77:426-432.
    • (1994) J Appl Bacteriol , vol.77 , pp. 426-432
    • McCarthy, S.A.1    Johnson, R.M.2    Kakimoto, D.3
  • 18
    • 46149107274 scopus 로고    scopus 로고
    • The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase
    • Gomez D., Espinosa E., Bertazzo M., Lucas-Elio P., Solano F., Sanchez-Amat A. The macromolecule with antimicrobial activity synthesized by Pseudoalteromonas luteoviolacea strains is an l-amino acid oxidase. Appl Microbiol Biotechnol 2008, 79:925-930.
    • (2008) Appl Microbiol Biotechnol , vol.79 , pp. 925-930
    • Gomez, D.1    Espinosa, E.2    Bertazzo, M.3    Lucas-Elio, P.4    Solano, F.5    Sanchez-Amat, A.6
  • 19
    • 0029741788 scopus 로고    scopus 로고
    • Purification and characterization of a novel antibacterial protein from marine bacterium D2
    • James S.G., Holmstrom C., Kjelleberg S. Purification and characterization of a novel antibacterial protein from marine bacterium D2. Appl Environ Microbiol 1996, 62:2783-2788.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 2783-2788
    • James, S.G.1    Holmstrom, C.2    Kjelleberg, S.3
  • 21
    • 33747360999 scopus 로고    scopus 로고
    • Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilm
    • Mai-Prochnow A., Weeb J.S., Ferrari B.C., Kjelleberg S. Ecological advantages of autolysis during the development and dispersal of Pseudoalteromonas tunicata biofilm. Appl Environ Microbiol 2006, 72:5414-5420.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 5414-5420
    • Mai-Prochnow, A.1    Weeb, J.S.2    Ferrari, B.C.3    Kjelleberg, S.4
  • 22
    • 48149097054 scopus 로고    scopus 로고
    • Hydrogen peroxide linked to lysine oxidase activity facilitates biofilm differentiation and dispersal in several Gram-negative bacteria
    • Mai-Prochnow A., Lucas-Elio P., Egan S., Thomas T., Webb J.S., Sanchez-Amat A., et al. Hydrogen peroxide linked to lysine oxidase activity facilitates biofilm differentiation and dispersal in several Gram-negative bacteria. J Bacteriol 2008, 190:5493-5501.
    • (2008) J Bacteriol , vol.190 , pp. 5493-5501
    • Mai-Prochnow, A.1    Lucas-Elio, P.2    Egan, S.3    Thomas, T.4    Webb, J.S.5    Sanchez-Amat, A.6
  • 23
    • 11844258204 scopus 로고    scopus 로고
    • Purification and partial characterization of marinocine, a new broad-spectrum antibacterial protein produced by Marinomonas mediterranea
    • Lucas-Elio P., Hernandez P., Sanchez-Amat A., Solano F. Purification and partial characterization of marinocine, a new broad-spectrum antibacterial protein produced by Marinomonas mediterranea. Biochim Biophys Acta 2005, 1721:193-203.
    • (2005) Biochim Biophys Acta , vol.1721 , pp. 193-203
    • Lucas-Elio, P.1    Hernandez, P.2    Sanchez-Amat, A.3    Solano, F.4
  • 24
    • 33645221476 scopus 로고    scopus 로고
    • The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity
    • Lucas-Elio P., Gomez D., Solano F., Sanchez-Amat A. The antimicrobial activity of marinocine, synthesized by Marinomonas mediterranea, is due to hydrogen peroxide generated by its lysine oxidase activity. J Bacteriol 2006, 188:2493-2501.
    • (2006) J Bacteriol , vol.188 , pp. 2493-2501
    • Lucas-Elio, P.1    Gomez, D.2    Solano, F.3    Sanchez-Amat, A.4
  • 26
    • 0036740805 scopus 로고    scopus 로고
    • Rheinheimera baltica gen. nov., sp. nov., a blue-coloured bacterium isolated from the central Baltic Sea
    • Brettar I., Christen R., Höfle M.G. Rheinheimera baltica gen. nov., sp. nov., a blue-coloured bacterium isolated from the central Baltic Sea. Int J Syst Evol Microbiol 2002, 52:1851-1857.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 1851-1857
    • Brettar, I.1    Christen, R.2    Höfle, M.G.3
  • 28
    • 33749015733 scopus 로고    scopus 로고
    • Rheinheimera perlucida sp. nov., a marine bacterium of the Gammaproteobacteria isolated from surface water of the central Baltic Sea
    • Brettar I., Christen R., Höfle M.G. Rheinheimera perlucida sp. nov., a marine bacterium of the Gammaproteobacteria isolated from surface water of the central Baltic Sea. Int J Syst Evol Microbiol 2006, 56:2177-2183.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 2177-2183
    • Brettar, I.1    Christen, R.2    Höfle, M.G.3
  • 29
    • 34547451077 scopus 로고    scopus 로고
    • Rheinheimera aquimaris sp. nov., isolated from seawater of the East Sea in Korea
    • Yoon J.H., Park S.E., Kang S.J., Oh T.K. Rheinheimera aquimaris sp. nov., isolated from seawater of the East Sea in Korea. Int J Syst Evol Microbiol 2007, 57:1386-1390.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 1386-1390
    • Yoon, J.H.1    Park, S.E.2    Kang, S.J.3    Oh, T.K.4
  • 30
    • 34548185222 scopus 로고    scopus 로고
    • Rheinheimera chironomi sp. nov., isolated from a chironomid (Diptera; Chironomidae) egg mass
    • Halpern M., Senderovich Y., Snir S. Rheinheimera chironomi sp. nov., isolated from a chironomid (Diptera; Chironomidae) egg mass. Int J Syst Evol Microbiol 2007, 57:1872-1875.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 1872-1875
    • Halpern, M.1    Senderovich, Y.2    Snir, S.3
  • 31
    • 35649022179 scopus 로고    scopus 로고
    • Rheinheimera texasensis sp. nov., a halointolerant freshwater oligotroph
    • Merchant M.M., Welsh A.K., McLean R.J.C. Rheinheimera texasensis sp. nov., a halointolerant freshwater oligotroph. Int J Syst Evol Microbiol 2007, 57:2376-2380.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 2376-2380
    • Merchant, M.M.1    Welsh, A.K.2    McLean, R.J.C.3
  • 34
    • 25144486755 scopus 로고    scopus 로고
    • Molecular diversity and ecology of microbial plankton
    • Giovannoni S.J., Stingl U. Molecular diversity and ecology of microbial plankton. Nature 2005, 437:343-348.
    • (2005) Nature , vol.437 , pp. 343-348
    • Giovannoni, S.J.1    Stingl, U.2
  • 35
    • 70350136705 scopus 로고    scopus 로고
    • Diversity of both the cultivable protease-producing bacteria and their extracellular proteases in the sediments of the south China
    • March
    • Zhou M.Y., Chen X.L., Zhao H.L., Dang H.Y., Luan X.W., Zhang X.Y., et al. Diversity of both the cultivable protease-producing bacteria and their extracellular proteases in the sediments of the south China. Microb Ecol 2009, (March).
    • (2009) Microb Ecol
    • Zhou, M.Y.1    Chen, X.L.2    Zhao, H.L.3    Dang, H.Y.4    Luan, X.W.5    Zhang, X.Y.6
  • 36
    • 0034801924 scopus 로고    scopus 로고
    • Ralstonia taiwanensis sp. nov., isolated from root nodules of Mimosa species and sputum of a cystic fibrosis patient
    • Chen W.M., Laevens S., Lee T.M., Coenye T., de Vos P., Mergeay M., et al. Ralstonia taiwanensis sp. nov., isolated from root nodules of Mimosa species and sputum of a cystic fibrosis patient. Int J Syst Evol Microbiol 2001, 51:1729-1735.
    • (2001) Int J Syst Evol Microbiol , vol.51 , pp. 1729-1735
    • Chen, W.M.1    Laevens, S.2    Lee, T.M.3    Coenye, T.4    de Vos, P.5    Mergeay, M.6
  • 37
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 1999, 41:95-98.
    • (1999) Nucleic Acids Symp Ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 38
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 2004, 5:150-163.
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 39
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997, 24:4876-4882.
    • (1997) Nucleic Acids Res , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 41
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for constructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for constructing phylogenetic trees. Mol Biol Evol 1987, 4:406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 42
    • 0019797407 scopus 로고
    • Evolutionary trees from DNA sequences: a maximum likelihood approach
    • Felsenstein J. Evolutionary trees from DNA sequences: a maximum likelihood approach. J Mol Evol 1981, 17:368-376.
    • (1981) J Mol Evol , vol.17 , pp. 368-376
    • Felsenstein, J.1
  • 43
    • 84963036271 scopus 로고
    • Quantitative phyletics and the evolution of anurans
    • Kluge A.G., Farris F.S. Quantitative phyletics and the evolution of anurans. Syst Zool 1969, 18:1-32.
    • (1969) Syst Zool , vol.18 , pp. 1-32
    • Kluge, A.G.1    Farris, F.S.2
  • 45
    • 35648991375 scopus 로고    scopus 로고
    • EzTaxon: a web-based tool for the identification of prokaryotes based on 16S ribosomal RNA gene sequences
    • Chun J., Lee J.-H., Jung Y., Kim M., Kim S., Kim B.K., et al. EzTaxon: a web-based tool for the identification of prokaryotes based on 16S ribosomal RNA gene sequences. Int J Syst Evol Microbiol 2007, 57:2259-2261.
    • (2007) Int J Syst Evol Microbiol , vol.57 , pp. 2259-2261
    • Chun, J.1    Lee, J.-H.2    Jung, Y.3    Kim, M.4    Kim, S.5    Kim, B.K.6
  • 47
    • 0002679069 scopus 로고
    • Procedures and theoretical considerations for testing antimicrobial agents in agar media
    • William & Wilkins, Baltimore, V. Logan (Ed.)
    • Barry A.I. Procedures and theoretical considerations for testing antimicrobial agents in agar media. Antibiotics in laboratory medicine 1980, 10-16. William & Wilkins, Baltimore. V. Logan (Ed.).
    • (1980) Antibiotics in laboratory medicine , pp. 10-16
    • Barry, A.I.1
  • 48
    • 0015076683 scopus 로고
    • Purification and properties of unicellular blue-green algae (order Chroococcales)
    • Stanier R.Y., Kunisawa R., Mandel M., Cohen-Bazire G. Purification and properties of unicellular blue-green algae (order Chroococcales). Bacteriol Rev 1971, 35:171-205.
    • (1971) Bacteriol Rev , vol.35 , pp. 171-205
    • Stanier, R.Y.1    Kunisawa, R.2    Mandel, M.3    Cohen-Bazire, G.4
  • 49
    • 34548864382 scopus 로고    scopus 로고
    • A novel agar medium to detect hydrogen peroxide-producing bacteria based on the Prussian blue-forming reaction
    • Saito M., Seki M., Iida K., Nakayama H., Yoshida S. A novel agar medium to detect hydrogen peroxide-producing bacteria based on the Prussian blue-forming reaction. Microbial Immunol 2007, 51:889-892.
    • (2007) Microbial Immunol , vol.51 , pp. 889-892
    • Saito, M.1    Seki, M.2    Iida, K.3    Nakayama, H.4    Yoshida, S.5
  • 50
    • 0021192882 scopus 로고
    • Determination of HDL-cholesterol using 2,4,6-tribromo-3-hydroxybenzoic acid with a commercial CHOD-PAP reagent
    • Trinder P., Webster D. Determination of HDL-cholesterol using 2,4,6-tribromo-3-hydroxybenzoic acid with a commercial CHOD-PAP reagent. Ann Clin Biochem 1984, 5:430-433.
    • (1984) Ann Clin Biochem , vol.5 , pp. 430-433
    • Trinder, P.1    Webster, D.2
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 52
    • 0019323979 scopus 로고
    • Some properties of a basic l-amino acid oxidase from Anacystis nidulans
    • Pistorius E.K., Voss H. Some properties of a basic l-amino acid oxidase from Anacystis nidulans. Biochim Biophys Acta 1980, 611:227-240.
    • (1980) Biochim Biophys Acta , vol.611 , pp. 227-240
    • Pistorius, E.K.1    Voss, H.2
  • 53
    • 0026759430 scopus 로고
    • Purification and some properties of an extracellular l-amino acid oxidase from Cellulomonas cellulans AM8 isolated from soil
    • Braun M., Kim J.M., Schmid R.D. Purification and some properties of an extracellular l-amino acid oxidase from Cellulomonas cellulans AM8 isolated from soil. Appl Microbiol Biotechnol 1992, 37:594-598.
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 594-598
    • Braun, M.1    Kim, J.M.2    Schmid, R.D.3
  • 54
    • 0028145168 scopus 로고
    • Purification and partial characterization of a broad-range l-amino acid oxidase from Bacillus carotarum 2Pfa isolated from soil
    • Brearley G.M., Price C.P., Atkinson T., Hammond P.M. Purification and partial characterization of a broad-range l-amino acid oxidase from Bacillus carotarum 2Pfa isolated from soil. Appl Microbiol Biotechnol 1994, 41:670-676.
    • (1994) Appl Microbiol Biotechnol , vol.41 , pp. 670-676
    • Brearley, G.M.1    Price, C.P.2    Atkinson, T.3    Hammond, P.M.4
  • 55
    • 0036644230 scopus 로고    scopus 로고
    • A new bacterial l-amino acid oxidase with a broad substrate specificity: purification and characterization
    • Geueke B., Hummel W. A new bacterial l-amino acid oxidase with a broad substrate specificity: purification and characterization. Enzyme Microb Technol 2002, 31:77-87.
    • (2002) Enzyme Microb Technol , vol.31 , pp. 77-87
    • Geueke, B.1    Hummel, W.2
  • 57
    • 0019434616 scopus 로고
    • L-Cysteine oxidase activity in the membrane of Neisseria meningitidis
    • Yu E.K.C., de Voe J.W. l-Cysteine oxidase activity in the membrane of Neisseria meningitidis. J Bacteriol 1980, 145:280-287.
    • (1980) J Bacteriol , vol.145 , pp. 280-287
    • Yu, E.K.C.1    de Voe, J.W.2
  • 58
    • 0020195726 scopus 로고
    • Purification and characterization of a novel l-phenylalanine oxidase (deaminating and decarboxylating) [from Pseudomonas sp. P-501]
    • Koyama H. Purification and characterization of a novel l-phenylalanine oxidase (deaminating and decarboxylating) [from Pseudomonas sp. P-501]. J Biochem 1982, 92:1235-1240.
    • (1982) J Biochem , vol.92 , pp. 1235-1240
    • Koyama, H.1
  • 59
  • 60
    • 0019960467 scopus 로고
    • Regulation of l-amino acid oxidase and of D-amino acid oxidase in Neurospora crassa
    • Sikora L., Marzluf G.A. Regulation of l-amino acid oxidase and of D-amino acid oxidase in Neurospora crassa. Mol Gen Genet 1982, 186:33-39.
    • (1982) Mol Gen Genet , vol.186 , pp. 33-39
    • Sikora, L.1    Marzluf, G.A.2
  • 61
    • 22144480320 scopus 로고    scopus 로고
    • Amino acid catabolism by an areA-regulated gene encoding an l-amino acid oxidase with broad substrate specificity in Aspergillus nidulans
    • Davis M.A., Askin M.C., Hynes M.J. Amino acid catabolism by an areA-regulated gene encoding an l-amino acid oxidase with broad substrate specificity in Aspergillus nidulans. Appl Environ Microbiol 2005, 71:3551-3555.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3551-3555
    • Davis, M.A.1    Askin, M.C.2    Hynes, M.J.3
  • 63
    • 0037018951 scopus 로고    scopus 로고
    • The commonality of risk factors for nosocomial colonization and infection with antimicrobial-resistant Staphylococcus aureus, enterococcus, gram-negative bacilli, Clostridium difficile, and Candida
    • Safdar N., Maki D.G. The commonality of risk factors for nosocomial colonization and infection with antimicrobial-resistant Staphylococcus aureus, enterococcus, gram-negative bacilli, Clostridium difficile, and Candida. Ann Intern Med 2002, 136:834-844.
    • (2002) Ann Intern Med , vol.136 , pp. 834-844
    • Safdar, N.1    Maki, D.G.2
  • 64
    • 77950341846 scopus 로고    scopus 로고
    • Vibrios as causal agents of zoonoses
    • March
    • Austin B. Vibrios as causal agents of zoonoses. Vet Microbiol 2009, (March).
    • (2009) Vet Microbiol
    • Austin, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.