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Volumn 5, Issue 6, 2012, Pages 700-716

Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: Close relationship to the Mycobacterium tuberculosis prodrug activator EtaA

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE; BAEYER VILLIGER MONOOXYGENASES; ETHIONAMIDE; ETHIONAMIDE MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 84867613558     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2012.00356.x     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0034186366 scopus 로고    scopus 로고
    • Prodrug activation enzymes in cancer gene therapy
    • Aghi, M., Hochberg, F., and Breakefield, X.O. (2000) Prodrug activation enzymes in cancer gene therapy. J Gene Med 2: 148-164.
    • (2000) J Gene Med , vol.2 , pp. 148-164
    • Aghi, M.1    Hochberg, F.2    Breakefield, X.O.3
  • 3
    • 0026745562 scopus 로고
    • The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) - I. Purification and properties of a nitroreductase enzyme from Escherichia coli - a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT)
    • Anlezark, G.M., Melton, R.G., Sherwood, R.F., Coles, B., Friedlos, F., and Knox, R.J. (1992) The bioactivation of 5-(aziridin-1-yl)-2, 4-dinitrobenzamide (CB 1954) - I. Purification and properties of a nitroreductase enzyme from Escherichia coli - a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT). Biochem Pharmacol 44: 2289-2295.
    • (1992) Biochem Pharmacol , vol.44 , pp. 2289-2295
    • Anlezark, G.M.1    Melton, R.G.2    Sherwood, R.F.3    Coles, B.4    Friedlos, F.5    Knox, R.J.6
  • 4
    • 66349089237 scopus 로고    scopus 로고
    • Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway
    • Beam, M.P., Bosserman, M.A., Noinaj, N., Wehenkel, M., and Rohr, J. (2009) Crystal structure of Baeyer-Villiger monooxygenase MtmOIV, the key enzyme of the mithramycin biosynthetic pathway. Biochemistry 48: 4476-4487.
    • (2009) Biochemistry , vol.48 , pp. 4476-4487
    • Beam, M.P.1    Bosserman, M.A.2    Noinaj, N.3    Wehenkel, M.4    Rohr, J.5
  • 5
    • 0026801560 scopus 로고
    • Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans
    • van Beilen, J.B., Penninga, D., and Witholt, B. (1992) Topology of the membrane-bound alkane hydroxylase of Pseudomonas oleovorans J Biol Chem 267: 9194-9201.
    • (1992) J Biol Chem , vol.267 , pp. 9194-9201
    • van Beilen, J.B.1    Penninga, D.2    Witholt, B.3
  • 7
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • van Berkel, W.J.H., Kamerbeek, N.M., and Fraaije, M.W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J Biotechnol 124: 670-689.
    • (2006) J Biotechnol , vol.124 , pp. 670-689
    • van Berkel, W.J.H.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 8
    • 80955145749 scopus 로고    scopus 로고
    • Bacterial metabolism of alkanes and ammonia under oxygen depleted conditions
    • Berthe-Corti, L., and Fetzner, S. (2002) Bacterial metabolism of alkanes and ammonia under oxygen depleted conditions. Acta Biotechnol 22: 299-336.
    • (2002) Acta Biotechnol , vol.22 , pp. 299-336
    • Berthe-Corti, L.1    Fetzner, S.2
  • 9
    • 84855816174 scopus 로고    scopus 로고
    • In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3
    • Catucci, G., Gilardi, G., Jeuken, L., and Sadeghi, S.J. (2012) In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3. Biochem Pharmacol 83: 551-558.
    • (2012) Biochem Pharmacol , vol.83 , pp. 551-558
    • Catucci, G.1    Gilardi, G.2    Jeuken, L.3    Sadeghi, S.J.4
  • 10
    • 1842268367 scopus 로고    scopus 로고
    • Involvement of His162 in NADPH binding of p-hydroxybenzoate hydroxylase
    • Mas-sey, K., and Williams, V. (eds). Calgary: University Press
    • Eppink, M.H.M., Jacobs, D., and van Berkel, W.J.H. (1997) Involvement of His162 in NADPH binding of p-hydroxybenzoate hydroxylase. In Flavins Andjlavoproteins XI Stevenson. Mas-sey, K., and Williams, V. (eds). Calgary: University Press, pp. 315-318.
    • (1997) Flavins Andjlavoproteins XI Stevenson , pp. 315-318
    • Eppink, M.H.M.1    van Jacobs, D.2    Berkel, W.J.H.3
  • 11
    • 34248385250 scopus 로고    scopus 로고
    • Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir
    • Feng, L., Wang, W., Cheng, J., Ren, Y., Zhao, G., Gao, C., etal. (2007) Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir. Proc Natl Acad Sci USA 104: 5602-5607.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5602-5607
    • Feng, L.1    Wang, W.2    Cheng, J.3    Ren, Y.4    Zhao, G.5    Gao, C.6
  • 12
  • 13
    • 0942287234 scopus 로고    scopus 로고
    • The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase
    • Fraaije, M.W., Kamerbeek, N.M., Heidekamp, A.J., Fortin, R., and Janssen, D.B. (2004) The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase. J Biol Chem 279: 3354-3360.
    • (2004) J Biol Chem , vol.279 , pp. 3354-3360
    • Fraaije, M.W.1    Kamerbeek, N.M.2    Heidekamp, A.J.3    Fortin, R.4    Janssen, D.B.5
  • 14
    • 0000265909 scopus 로고
    • Biological routes to optically active epoxides
    • Collins, A.N., Sheldrake, G.N., and Crosby, J. (eds). London, UK: John Wiley & Sons
    • Furuhashi, K. (1992) Biological routes to optically active epoxides. In Chirality in Industry. Collins, A.N., Sheldrake, G.N., and Crosby, J. (eds). London, UK: John Wiley & Sons, pp. 167-186.
    • (1992) Chirality in Industry , pp. 167-186
    • Furuhashi, K.1
  • 15
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: applications of autodock
    • Goodsell, D.S., Morris, G.M., and Olson, A.J. (1996) Automated docking of flexible ligands: applications of autodock. J Mol Recognit 9: 1-5.
    • (1996) J Mol Recognit , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 16
    • 0035123128 scopus 로고    scopus 로고
    • Gene directed enzyme/prodrug therapy of cancer: historical appraisal and future prospectives
    • Greco, O., and Dachs, G.U. (2001) Gene directed enzyme/prodrug therapy of cancer: historical appraisal and future prospectives. J Cell Physiol 187: 22-36.
    • (2001) J Cell Physiol , vol.187 , pp. 22-36
    • Greco, O.1    Dachs, G.U.2
  • 17
    • 0026802983 scopus 로고
    • A monoclonal antibody-beta-glucuronidase conjugate as activator of the prodrug epirubicin-glucuronide for specific treatment of cancer
    • Haisma, H.J., Boven, E., van Muijen, M., de Jong, J., van der Vijgh, W.J., and Pinedo, H.M. (1992) A monoclonal antibody-beta-glucuronidase conjugate as activator of the prodrug epirubicin-glucuronide for specific treatment of cancer. Br J Cancer 66: 474-478.
    • (1992) Br J Cancer , vol.66 , pp. 474-478
    • Haisma, H.J.1    van Boven, E.2    de Muijen, M.3    van der Jong, J.4    Vijgh, W.J.5    Pinedo, H.M.6
  • 18
    • 0019296687 scopus 로고
    • A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences
    • Kimura, M. (1980) A simple method for estimating evolutionary rate of base substitutions through comparative studies of nucleotide sequences. J Mol Evol 16: 111-120.
    • (1980) J Mol Evol , vol.16 , pp. 111-120
    • Kimura, M.1
  • 19
    • 78651287426 scopus 로고    scopus 로고
    • DrugBank 3.0: a comprehensive resource for 'omics' research on drugs
    • Knox, C., Law, V., Jewison, T., Liu, P., Ly, S., Frolkis, A., etal. (2011) DrugBank 3.0: a comprehensive resource for 'omics' research on drugs. Nucleic Acids Res 39: D1035-D1041.
    • (2011) Nucleic Acids Res , vol.39
    • Knox, C.1    Law, V.2    Jewison, T.3    Liu, P.4    Ly, S.5    Frolkis, A.6
  • 20
    • 0035117021 scopus 로고    scopus 로고
    • Biodegradation of long-chain n-paraffins from waste oil of car engine by Acinetobacter sp
    • Koma, D., Hasumi, F., Yamamoto, E., Ohta, T., Chung, S.-Y., and Kubo, M. (2001) Biodegradation of long-chain n-paraffins from waste oil of car engine by Acinetobacter sp. J Biosci Bioeng 91: 94-96.
    • (2001) J Biosci Bioeng , vol.91 , pp. 94-96
    • Koma, D.1    Hasumi, F.2    Yamamoto, E.3    Ohta, T.4    Chung, S.-Y.5    Kubo, M.6
  • 21
    • 33846578243 scopus 로고    scopus 로고
    • Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp. strain TY-5
    • Kotani, T., Yurimoto, H., Kato, N., and Sakai, Y. (2007) Novel acetone metabolism in a propane-utilizing bacterium, Gordonia sp. strain TY-5. J Bacteriol 189: 886-889.
    • (2007) J Bacteriol , vol.189 , pp. 886-889
    • Kotani, T.1    Yurimoto, H.2    Kato, N.3    Sakai, Y.4
  • 22
    • 0036191007 scopus 로고    scopus 로고
    • Model@Home: distributed computing in bioinformatics using a screensaver based approach
    • Krieger, E., and Vriend, A. (2002) Model@Home: distributed computing in bioinformatics using a screensaver based approach. Bioinformatics 18: 315-318.
    • (2002) Bioinformatics , vol.18 , pp. 315-318
    • Krieger, E.1    Vriend, A.2
  • 23
    • 0037198618 scopus 로고    scopus 로고
    • Understanding and exploiting C-H bond activation
    • Labinger, J.A., and Bercaw, J.E. (2002) Understanding and exploiting C-H bond activation. Nature 417: 507-514.
    • (2002) Nature , vol.417 , pp. 507-514
    • Labinger, J.A.1    Bercaw, J.E.2
  • 24
    • 0000243829 scopus 로고
    • procheck: a program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993) procheck: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 38349124762 scopus 로고    scopus 로고
    • Crystal structure of long-chain alakane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alane hydroxylase
    • Li, L., Liu, X., Yang, W., Xu, F., Wang, W., Feng, L., etal. (2008) Crystal structure of long-chain alakane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alane hydroxylase. J Mol Biol 376: 453-465.
    • (2008) J Mol Biol , vol.376 , pp. 453-465
    • Li, L.1    Liu, X.2    Yang, W.3    Xu, F.4    Wang, W.5    Feng, L.6
  • 26
    • 79955013063 scopus 로고    scopus 로고
    • Multiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5
    • Liu, C., Wang, W., Wu, Y., Zhou, Z., and Lai, Q. (2011) Multiple alkane hydroxylase systems in a marine alkane degrader, Alcanivorax dieselolei B-5. Environ Microbiol 13: 1168-1178.
    • (2011) Environ Microbiol , vol.13 , pp. 1168-1178
    • Liu, C.1    Wang, W.2    Wu, Y.3    Zhou, Z.4    Lai, Q.5
  • 27
    • 0038534422 scopus 로고    scopus 로고
    • Isolation and characterization of a novel oxygenase that catalyzes the first step of n-alkane oxidation in Acinetobacter sp. strain M-1
    • Maeng, J.H., Sakai, Y., Tani, Y., and Kato, N. (1996) Isolation and characterization of a novel oxygenase that catalyzes the first step of n-alkane oxidation in Acinetobacter sp. strain M-1. J Bacteriol 178: 3695-3700.
    • (1996) J Bacteriol , vol.178 , pp. 3695-3700
    • Maeng, J.H.1    Sakai, Y.2    Tani, Y.3    Kato, N.4
  • 28
    • 0034801865 scopus 로고    scopus 로고
    • Molecular characterization of the 56-kDA CYP153 from Acinetobacter sp. EB104
    • Maier, T., Förster, H.H., Asperger, O., and Hahn, U. (2001) Molecular characterization of the 56-kDA CYP153 from Acinetobacter sp. EB104. Biochem Biophys Res Commun 286: 652-658.
    • (2001) Biochem Biophys Res Commun , vol.286 , pp. 652-658
    • Maier, T.1    Förster, H.H.2    Asperger, O.3    Hahn, U.4
  • 30
    • 67649607265 scopus 로고    scopus 로고
    • Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor
    • Mirza, I.A., Yachnin, B.J., Wang, S., Grosse, S., Bergeron, H., Imura, A., etal. (2009) Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor. J Am Chem Soc 131: 8848-8854.
    • (2009) J Am Chem Soc , vol.131 , pp. 8848-8854
    • Mirza, I.A.1    Yachnin, B.J.2    Wang, S.3    Grosse, S.4    Bergeron, H.5    Imura, A.6
  • 31
    • 0024328202 scopus 로고
    • Purification of cytochrome P-450 from n-hexadecane-grown Acinetobacter calcoaceticus
    • Muller, R., Asperger, O., and Kleber, H.P. (1989) Purification of cytochrome P-450 from n-hexadecane-grown Acinetobacter calcoaceticus Biomed Biochim Acta 48: 243-254.
    • (1989) Biomed Biochim Acta , vol.48 , pp. 243-254
    • Muller, R.1    Asperger, O.2    Kleber, H.P.3
  • 32
    • 0030630176 scopus 로고    scopus 로고
    • Acinetobacter radioresistens metabolizing aromatic compounds. Biochemical and microbiological characterization of the strain
    • Pessione, E., and Giunta, C. (1997) Acinetobacter radioresistens metabolizing aromatic compounds. Biochemical and microbiological characterization of the strain. Microbios 89: 105-117.
    • (1997) Microbios , vol.89 , pp. 105-117
    • Pessione, E.1    Giunta, C.2
  • 33
    • 34547630476 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440
    • Rehdorf, J., Kirschner, A., and Bornscheuer, U.T. (2007) Cloning, expression and characterization of a Baeyer-Villiger monooxygenase from Pseudomonas putida KT2440. Biotechnol Lett 29: 1393-1398.
    • (2007) Biotechnol Lett , vol.29 , pp. 1393-1398
    • Rehdorf, J.1    Kirschner, A.2    Bornscheuer, U.T.3
  • 34
    • 70349655393 scopus 로고    scopus 로고
    • Degradation of alkanes by bacteria
    • Rojo, F. (2009) Degradation of alkanes by bacteria. Environ Microbiol 11: 2477-2490.
    • (2009) Environ Microbiol , vol.11 , pp. 2477-2490
    • Rojo, F.1
  • 35
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou, N., and Nei, M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4: 406-425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 36
    • 0001417645 scopus 로고
    • Use of long-chain n-alkanes (C13-C44) by an isolate, Acinetobacter sp. M-1
    • Sakai, Y., Maeng, J.H., Tani, Y., and Kato, N. (1994) Use of long-chain n-alkanes (C13-C44) by an isolate, Acinetobacter sp. M-1. Biosci Biotechnol Biochem 58: 2128-2130.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 2128-2130
    • Sakai, Y.1    Maeng, J.H.2    Tani, Y.3    Kato, N.4
  • 38
    • 0028089687 scopus 로고
    • Eight histidine residues are catalytically essential in a membrane associated iron enzyme, stearoyl-CoA desaturase and are conserved in alkane hydroxylase and xylene monooxygenase
    • Shanklin, J., Whittle, E., and Fox, B.G. (1994) Eight histidine residues are catalytically essential in a membrane associated iron enzyme, stearoyl-CoA desaturase and are conserved in alkane hydroxylase and xylene monooxygenase. Biochemistry 33: 12787-12794.
    • (1994) Biochemistry , vol.33 , pp. 12787-12794
    • Shanklin, J.1    Whittle, E.2    Fox, B.G.3
  • 39
    • 0026900387 scopus 로고
    • Human immune response to monoclonal antibody-enzyme conjugates in ADEPT pilot clinical trial
    • Sharma, S.K., Bagshawe, K.D., Melton, R.G., and Sherwood, R.F. (1992) Human immune response to monoclonal antibody-enzyme conjugates in ADEPT pilot clinical trial. Cell Biophys 21: 109-120.
    • (1992) Cell Biophys , vol.21 , pp. 109-120
    • Sharma, S.K.1    Bagshawe, K.D.2    Melton, R.G.3    Sherwood, R.F.4
  • 40
    • 0031596383 scopus 로고    scopus 로고
    • Cancer chemotherapy using suicide genes
    • Singhal, S., and Kaiser, L.R. (1998) Cancer chemotherapy using suicide genes. Surg Oncol Clin N Am 7: 505-536.
    • (1998) Surg Oncol Clin N Am , vol.7 , pp. 505-536
    • Singhal, S.1    Kaiser, L.R.2
  • 41
    • 0033171433 scopus 로고    scopus 로고
    • Molecular screening for alkane hydroxylase genes in Gram-negative and Gram-positive strains
    • Smits, T.H.M., Röthlisberger, M., Witholt, B., and van Beilen, J.B. (1999) Molecular screening for alkane hydroxylase genes in Gram-negative and Gram-positive strains. Environ Microbiol 1: 307-318.
    • (1999) Environ Microbiol , vol.1 , pp. 307-318
    • Smits, T.H.M.1    Röthlisberger, M.2    van Witholt, B.3    Beilen, J.B.4
  • 42
    • 0033732739 scopus 로고    scopus 로고
    • Prodrug/drug sensitivity gene therapy: current status
    • Smythe, W.R. (2000) Prodrug/drug sensitivity gene therapy: current status. Curr Oncol Rep 2: 17-22.
    • (2000) Curr Oncol Rep , vol.2 , pp. 17-22
    • Smythe, W.R.1
  • 43
    • 0028044090 scopus 로고
    • Frequency of genes in aromatic and aliphatic hydrocarbon biodegradation pathways within bacterial populations from Alaskan sediments
    • Sotsky, J.B., Greer, C.W., and Atlas, R.M. (1994) Frequency of genes in aromatic and aliphatic hydrocarbon biodegradation pathways within bacterial populations from Alaskan sediments. Can J Microbiol 40: 981-985.
    • (1994) Can J Microbiol , vol.40 , pp. 981-985
    • Sotsky, J.B.1    Greer, C.W.2    Atlas, R.M.3
  • 44
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24: 1596-1599.
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 45
    • 33747720825 scopus 로고    scopus 로고
    • Utilization of n-alkanes by a newly isolated strain of Acinetobacter venetianus: the role of two AlkB-type alkane hydroxylases
    • Throne-Holst, M., Markussen, S., Winnberg, A., Ellingsen, T.E., Kotlar, H.K., and Zotchev, S.B. (2006) Utilization of n-alkanes by a newly isolated strain of Acinetobacter venetianus: the role of two AlkB-type alkane hydroxylases. Appl Microbiol Biotechnol 72: 353-360.
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 353-360
    • Throne-Holst, M.1    Markussen, S.2    Winnberg, A.3    Ellingsen, T.E.4    Kotlar, H.K.5    Zotchev, S.B.6
  • 46
    • 34249658423 scopus 로고    scopus 로고
    • Identification of novel genes involved in long-chain n-alkane degradation by Acinetobacter sp. strain DSM 17874
    • Throne-Holst, M., Wentzel, A., Ellingsen, T.E., Kotlar, H.K., and Zotchev, S.B. (2007) Identification of novel genes involved in long-chain n-alkane degradation by Acinetobacter sp. strain DSM 17874. Appl Environ Microbiol 73: 3327-3332.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 3327-3332
    • Throne-Holst, M.1    Wentzel, A.2    Ellingsen, T.E.3    Kotlar, H.K.4    Zotchev, S.B.5
  • 47
    • 0347478284 scopus 로고    scopus 로고
    • Recent advances in petroleum microbiology and molecular biology
    • Van Hamme, J.D., Singh, A., and Ward, O.P. (2003) Recent advances in petroleum microbiology and molecular biology. Microbiology 67: 503-549.
    • (2003) Microbiology , vol.67 , pp. 503-549
    • Van Hamme, J.D.1    Singh, A.2    Ward, O.P.3
  • 48
    • 0037066702 scopus 로고    scopus 로고
    • The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase
    • Vannelli, T., Dykman, A., and Ortiz de Montellano, P. (2002) The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase. J Biol Chem 277: 12824-12829.
    • (2002) J Biol Chem , vol.277 , pp. 12824-12829
    • Vannelli, T.1    Dykman, A.2    Ortiz de Montellano, P.3
  • 49
    • 0026067797 scopus 로고
    • 16S ribosomal DNA amplification for phylogenetic study
    • Weisburg, W.G.S., Barns, M., Pelletier, D.A., and Lane, D.J. (1991) 16S ribosomal DNA amplification for phylogenetic study. J Bacteriol 173: 697-703.
    • (1991) J Bacteriol , vol.173 , pp. 697-703
    • Weisburg, W.G.S.1    Barns, M.2    Pelletier, D.A.3    Lane, D.J.4


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