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Volumn 6, Issue 11, 2017, Pages 2145-2156

Construction of Recombinant Pdu Metabolosome Shells for Small Molecule Production in Corynebacterium glutamicum

Author keywords

bacterial microcompartments; C. glutamicum; metabolic engineering; propanediol utilization; protein encapsulation

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE DEHYDROGENASE; BACTERIAL DNA; BACTERIAL PROTEIN; PDZ PROTEIN; PROPYLENE GLYCOL; PROTEIN GBD; PROTEIN SH3; PYRUVATE DECARBOXYLASE; RECOMBINANT DNA; UNCLASSIFIED DRUG;

EID: 85034585113     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.7b00167     Document Type: Article
Times cited : (34)

References (53)
  • 1
    • 84928138623 scopus 로고    scopus 로고
    • Engineering bacterial microcompartment shells: Chimeric shell proteins and chimeric carboxysome shells
    • Cai, F., Sutter, M., Bernstein, S. L., Kinney, J. N., and Kerfeld, C. A. (2015) Engineering bacterial microcompartment shells: chimeric shell proteins and chimeric carboxysome shells ACS Synth. Biol. 4, 444-453 10.1021/sb500226j
    • (2015) ACS Synth. Biol. , vol.4 , pp. 444-453
    • Cai, F.1    Sutter, M.2    Bernstein, S.L.3    Kinney, J.N.4    Kerfeld, C.A.5
  • 2
    • 84920531816 scopus 로고    scopus 로고
    • Bacterial microcompartments and the modular construction of microbial metabolism
    • Kerfeld, C. A. and Erbilgin, O. (2015) Bacterial microcompartments and the modular construction of microbial metabolism Trends Microbiol. 23, 22-34 10.1016/j.tim.2014.10.003
    • (2015) Trends Microbiol. , vol.23 , pp. 22-34
    • Kerfeld, C.A.1    Erbilgin, O.2
  • 3
    • 84960974974 scopus 로고    scopus 로고
    • Assembly, function and evolution of cyanobacterial carboxysomes
    • Kerfeld, C. A. and Melnicki, M. R. (2016) Assembly, function and evolution of cyanobacterial carboxysomes Curr. Opin. Plant Biol. 31, 66-75 10.1016/j.pbi.2016.03.009
    • (2016) Curr. Opin. Plant Biol. , vol.31 , pp. 66-75
    • Kerfeld, C.A.1    Melnicki, M.R.2
  • 4
    • 84874058227 scopus 로고    scopus 로고
    • Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria
    • Jorda, J., Lopez, D., Wheatley, N. M., and Yeates, T. O. (2013) Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria Protein Sci. 22, 179-195 10.1002/pro.2196
    • (2013) Protein Sci. , vol.22 , pp. 179-195
    • Jorda, J.1    Lopez, D.2    Wheatley, N.M.3    Yeates, T.O.4
  • 5
    • 0036178889 scopus 로고    scopus 로고
    • PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2
    • Havemann, G. D., Sampson, E. M., and Bobik, T. A. (2002) PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2 J. Bacteriol. 184, 1253-1261 10.1128/JB.184.5.1253-1261.2002
    • (2002) J. Bacteriol. , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 6
    • 84872197140 scopus 로고    scopus 로고
    • Bacterial microcompartments moving into a synthetic biological world
    • Frank, S., Lawrence, A. D., Prentice, M. B., and Warren, M. J. (2013) Bacterial microcompartments moving into a synthetic biological world J. Biotechnol. 163, 273-279 10.1016/j.jbiotec.2012.09.002
    • (2013) J. Biotechnol. , vol.163 , pp. 273-279
    • Frank, S.1    Lawrence, A.D.2    Prentice, M.B.3    Warren, M.J.4
  • 7
    • 78549246253 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell
    • Crowley, C. S., Cascio, D., Sawaya, M. R., Kopstein, J. S., Bobik, T. A., and Yeates, T. O. (2010) Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell J. Biol. Chem. 285, 37838-37846 10.1074/jbc.M110.160580
    • (2010) J. Biol. Chem. , vol.285 , pp. 37838-37846
    • Crowley, C.S.1    Cascio, D.2    Sawaya, M.R.3    Kopstein, J.S.4    Bobik, T.A.5    Yeates, T.O.6
  • 8
    • 84943455873 scopus 로고    scopus 로고
    • An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein
    • Thompson, M. C., Cascio, D., Leibly, D. J., and Yeates, T. O. (2015) An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein Protein Sci. 24, 956-975 10.1002/pro.2672
    • (2015) Protein Sci. , vol.24 , pp. 956-975
    • Thompson, M.C.1    Cascio, D.2    Leibly, D.J.3    Yeates, T.O.4
  • 9
    • 74849140487 scopus 로고    scopus 로고
    • Structure and mechanisms of a protein-based organelle in Escherichia coli
    • Tanaka, S., Sawaya, M. R., and Yeates, T. O. (2010) Structure and mechanisms of a protein-based organelle in Escherichia coli Science 327, 81-84 10.1126/science.1179513
    • (2010) Science , vol.327 , pp. 81-84
    • Tanaka, S.1    Sawaya, M.R.2    Yeates, T.O.3
  • 10
    • 0036178889 scopus 로고    scopus 로고
    • PduA is a shell protein of polyhedral organelles involved in coenzyme B-12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2
    • Havemann, G. D., Sampson, E. M., and Bobik, T. A. (2002) PduA is a shell protein of polyhedral organelles involved in coenzyme B-12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2 J. Bacteriol. 184, 1253-1261 10.1128/JB.184.5.1253-1261.2002
    • (2002) J. Bacteriol. , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 13
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
    • Parsons, J. B., Frank, S., Bhella, D., Liang, M., Prentice, M. B., Mulvihill, D. P., and Warren, M. J. (2010) Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement Mol. Cell 38, 305-315 10.1016/j.molcel.2010.04.008
    • (2010) Mol. Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1    Frank, S.2    Bhella, D.3    Liang, M.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 14
    • 84964403647 scopus 로고    scopus 로고
    • Engineering formation of multiple recombinant Eut protein nanocompartments in E. Coli
    • Held, M., Kolb, A., Perdue, S., Hsu, S. Y., Bloch, S. E., Quin, M. B., and Schmidt-Dannert, C. (2016) Engineering formation of multiple recombinant Eut protein nanocompartments in E. coli Sci. Rep. 6, 24359 10.1038/srep24359
    • (2016) Sci. Rep. , vol.6 , pp. 24359
    • Held, M.1    Kolb, A.2    Perdue, S.3    Hsu, S.Y.4    Bloch, S.E.5    Quin, M.B.6    Schmidt-Dannert, C.7
  • 15
    • 84858009996 scopus 로고    scopus 로고
    • Engineered protein nano-compartments for targeted enzyme localization
    • Choudhary, S., Quin, M. B., Sanders, M. A., Johnson, E. T., and Schmidt-Dannert, C. (2012) Engineered protein nano-compartments for targeted enzyme localization PLoS One 7, e33342 10.1371/journal.pone.0033342
    • (2012) PLoS One , vol.7 , pp. e33342
    • Choudhary, S.1    Quin, M.B.2    Sanders, M.A.3    Johnson, E.T.4    Schmidt-Dannert, C.5
  • 16
    • 84899945180 scopus 로고    scopus 로고
    • Assembly of robust bacterial microcompartment shells using building blocks from an organelle of unknown function
    • Lassila, J. K., Bernstein, S. L., Kinney, J. N., Axen, S. D., and Kerfeld, C. A. (2014) Assembly of robust bacterial microcompartment shells using building blocks from an organelle of unknown function J. Mol. Biol. 426, 2217-2228 10.1016/j.jmb.2014.02.025
    • (2014) J. Mol. Biol. , vol.426 , pp. 2217-2228
    • Lassila, J.K.1    Bernstein, S.L.2    Kinney, J.N.3    Axen, S.D.4    Kerfeld, C.A.5
  • 18
    • 84861208627 scopus 로고    scopus 로고
    • Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly
    • Kinney, J. N., Salmeen, A., Cai, F., and Kerfeld, C. A. (2012) Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly J. Biol. Chem. 287, 17729-17736 10.1074/jbc.M112.355305
    • (2012) J. Biol. Chem. , vol.287 , pp. 17729-17736
    • Kinney, J.N.1    Salmeen, A.2    Cai, F.3    Kerfeld, C.A.4
  • 20
    • 84866280237 scopus 로고    scopus 로고
    • Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
    • Fan, C., Cheng, S., Sinha, S., and Bobik, T. A. (2012) Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments Proc. Natl. Acad. Sci. U. S. A. 109, 14995-15000 10.1073/pnas.1207516109
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 14995-15000
    • Fan, C.1    Cheng, S.2    Sinha, S.3    Bobik, T.A.4
  • 21
    • 84961244390 scopus 로고    scopus 로고
    • Employing bacterial microcompartment technology to engineer a shell-free enzyme-aggregate for enhanced 1,2-propanediol production in Escherichia coli
    • Lee, M. J., Brown, I. R., Juodeikis, R., Frank, S., and Warren, M. J. (2016) Employing bacterial microcompartment technology to engineer a shell-free enzyme-aggregate for enhanced 1,2-propanediol production in Escherichia coli Metab. Eng. 36, 48-56 10.1016/j.ymben.2016.02.007
    • (2016) Metab. Eng. , vol.36 , pp. 48-56
    • Lee, M.J.1    Brown, I.R.2    Juodeikis, R.3    Frank, S.4    Warren, M.J.5
  • 22
    • 85012190873 scopus 로고    scopus 로고
    • Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. Coli
    • Liang, M., Frank, S., Lunsdorf, H., Warren, M. J., and Prentice, M. B. (2017) Bacterial microcompartment-directed polyphosphate kinase promotes stable polyphosphate accumulation in E. coli Biotechnol. J. 12, 10 10.1002/biot.201600415
    • (2017) Biotechnol. J. , vol.12 , pp. 10
    • Liang, M.1    Frank, S.2    Lunsdorf, H.3    Warren, M.J.4    Prentice, M.B.5
  • 23
    • 85018626807 scopus 로고    scopus 로고
    • Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein e from bacteriophage X174 in Escherichia coli
    • Yung, M. C., Bourguet, F. A., Carpenter, T. S., and Coleman, M. A. (2017) Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein E from bacteriophage X174 in Escherichia coli Microb. Cell Fact. 16, 71 10.1186/s12934-017-0685-x
    • (2017) Microb. Cell Fact. , vol.16 , pp. 71
    • Yung, M.C.1    Bourguet, F.A.2    Carpenter, T.S.3    Coleman, M.A.4
  • 24
    • 84969786353 scopus 로고    scopus 로고
    • The Actinobacterium Corynebacterium glutamicum, an Industrial Workhorse
    • Lee, J. Y., Na, Y. A., Kim, E., Lee, H. S., and Kim, P. (2016) The Actinobacterium Corynebacterium glutamicum, an Industrial Workhorse J. Microbiol. Biotechnol. 26, 807-822 10.4014/jmb.1601.01053
    • (2016) J. Microbiol. Biotechnol. , vol.26 , pp. 807-822
    • Lee, J.Y.1    Na, Y.A.2    Kim, E.3    Lee, H.S.4    Kim, P.5
  • 25
    • 84923868543 scopus 로고    scopus 로고
    • Advanced biotechnology: Metabolically engineered cells for the bio-based production of chemicals and fuels, materials, and health-care products
    • Becker, J. and Wittmann, C. (2015) Advanced biotechnology: metabolically engineered cells for the bio-based production of chemicals and fuels, materials, and health-care products Angew. Chem., Int. Ed. 54, 3328-3350 10.1002/anie.201409033
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 3328-3350
    • Becker, J.1    Wittmann, C.2
  • 26
    • 84905867273 scopus 로고    scopus 로고
    • Structural insights into higher order assembly and function of the bacterial microcompartment protein PduA
    • Pang, A., Frank, S., Brown, I., Warren, M. J., and Pickersgill, R. W. (2014) Structural insights into higher order assembly and function of the bacterial microcompartment protein PduA J. Biol. Chem. 289, 22377-22384 10.1074/jbc.M114.569285
    • (2014) J. Biol. Chem. , vol.289 , pp. 22377-22384
    • Pang, A.1    Frank, S.2    Brown, I.3    Warren, M.J.4    Pickersgill, R.W.5
  • 28
    • 0042389658 scopus 로고    scopus 로고
    • Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • Havemann, G. D. and Bobik, T. A. (2003) Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2 J. Bacteriol. 185, 5086-5095 10.1128/JB.185.17.5086-5095.2003
    • (2003) J. Bacteriol. , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 29
    • 84942086056 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for the production of itaconate
    • Otten, A., Brocker, M., and Bott, M. (2015) Metabolic engineering of Corynebacterium glutamicum for the production of itaconate Metab. Eng. 30, 156-165 10.1016/j.ymben.2015.06.003
    • (2015) Metab. Eng. , vol.30 , pp. 156-165
    • Otten, A.1    Brocker, M.2    Bott, M.3
  • 30
    • 79952367508 scopus 로고    scopus 로고
    • Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella
    • Cheng, S., Sinha, S., Fan, C., Liu, Y., and Bobik, T. A. (2011) Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella J. Bacteriol. 193, 1385-1392 10.1128/JB.01473-10
    • (2011) J. Bacteriol. , vol.193 , pp. 1385-1392
    • Cheng, S.1    Sinha, S.2    Fan, C.3    Liu, Y.4    Bobik, T.A.5
  • 31
    • 84913534836 scopus 로고    scopus 로고
    • Engineering transcriptional regulation to control Pdu microcompartment formation
    • Kim, E. Y., Jakobson, C. M., and Tullman-Ercek, D. (2014) Engineering transcriptional regulation to control Pdu microcompartment formation PLoS One 9, e113814 10.1371/journal.pone.0113814
    • (2014) PLoS One , vol.9 , pp. e113814
    • Kim, E.Y.1    Jakobson, C.M.2    Tullman-Ercek, D.3
  • 32
    • 84873966152 scopus 로고    scopus 로고
    • Destabilized eYFP variants for dynamic gene expression studies in Corynebacterium glutamicum
    • Hentschel, E., Will, C., Mustafi, N., Burkovski, A., Rehm, N., and Frunzke, J. (2013) Destabilized eYFP variants for dynamic gene expression studies in Corynebacterium glutamicum Microb. Biotechnol. 6, 196-201 10.1111/j.1751-7915.2012.00360.x
    • (2013) Microb. Biotechnol. , vol.6 , pp. 196-201
    • Hentschel, E.1    Will, C.2    Mustafi, N.3    Burkovski, A.4    Rehm, N.5    Frunzke, J.6
  • 33
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman, C., Thevenet, D., Bouloc, P., Walker, G. C., and D'Ari, R. (1998) Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH) Genes Dev. 12, 1348-1355 10.1101/gad.12.9.1348
    • (1998) Genes Dev. , vol.12 , pp. 1348-1355
    • Herman, C.1    Thevenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 35
    • 34547113519 scopus 로고    scopus 로고
    • Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase
    • Orita, I., Sakamoto, N., Kato, N., Yurimoto, H., and Sakai, Y. (2007) Bifunctional enzyme fusion of 3-hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase Appl. Microbiol. Biotechnol. 76, 439-445 10.1007/s00253-007-1023-8
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 439-445
    • Orita, I.1    Sakamoto, N.2    Kato, N.3    Yurimoto, H.4    Sakai, Y.5
  • 36
    • 0037133537 scopus 로고    scopus 로고
    • Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway
    • James, C. L. and Viola, R. E. (2002) Production and characterization of bifunctional enzymes. Substrate channeling in the aspartate pathway Biochemistry 41, 3726-3731 10.1021/bi0159074
    • (2002) Biochemistry , vol.41 , pp. 3726-3731
    • James, C.L.1    Viola, R.E.2
  • 37
    • 84869875863 scopus 로고    scopus 로고
    • Designing biological compartmentalization
    • Chen, A. H. and Silver, P. A. (2012) Designing biological compartmentalization Trends Cell Biol. 22, 662-670 10.1016/j.tcb.2012.07.002
    • (2012) Trends Cell Biol. , vol.22 , pp. 662-670
    • Chen, A.H.1    Silver, P.A.2
  • 38
    • 84859780045 scopus 로고    scopus 로고
    • Spatial organization of enzymes for metabolic engineering
    • Lee, H., DeLoache, W. C., and Dueber, J. E. (2012) Spatial organization of enzymes for metabolic engineering Metab. Eng. 14, 242-251 10.1016/j.ymben.2011.09.003
    • (2012) Metab. Eng. , vol.14 , pp. 242-251
    • Lee, H.1    DeLoache, W.C.2    Dueber, J.E.3
  • 39
    • 25444479070 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions
    • Inui, M., Kawaguchi, H., Murakami, S., Vertes, A. A., and Yukawa, H. (2004) Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions J. Mol. Microbiol. Biotechnol. 8, 243-254 10.1159/000086705
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.8 , pp. 243-254
    • Inui, M.1    Kawaguchi, H.2    Murakami, S.3    Vertes, A.A.4    Yukawa, H.5
  • 40
    • 85026661870 scopus 로고    scopus 로고
    • Heterologous expression of the Halothiobacillus neapolitanus carboxysomal gene cluster in Corynebacterium glutamicum
    • Baumgart, M., Huber, I., Abdollahzadeh, I., Gensch, T., and Frunzke, J. (2017) Heterologous expression of the Halothiobacillus neapolitanus carboxysomal gene cluster in Corynebacterium glutamicum J. Biotechnol. 27, 30124-30124 10.1016/j.jbiotec.2017.03.019
    • (2017) J. Biotechnol. , vol.27 , pp. 30124
    • Baumgart, M.1    Huber, I.2    Abdollahzadeh, I.3    Gensch, T.4    Frunzke, J.5
  • 41
    • 85019592121 scopus 로고    scopus 로고
    • CipA and CipB as scaffolds to organize proteins into crystalline inclusions
    • Wang, Y., Heermann, R., and Jung, K. (2017) CipA and CipB as scaffolds to organize proteins into crystalline inclusions ACS Synth. Biol. 6, 826 10.1021/acssynbio.6b00323
    • (2017) ACS Synth. Biol. , vol.6 , pp. 826
    • Wang, Y.1    Heermann, R.2    Jung, K.3
  • 42
    • 77950863739 scopus 로고    scopus 로고
    • Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. Coli
    • Moon, T. S., Dueber, J. E., Shiue, E., and Prather, K. L. (2010) Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli Metab. Eng. 12, 298-305 10.1016/j.ymben.2010.01.003
    • (2010) Metab. Eng. , vol.12 , pp. 298-305
    • Moon, T.S.1    Dueber, J.E.2    Shiue, E.3    Prather, K.L.4
  • 43
    • 84994494330 scopus 로고    scopus 로고
    • Scaffoldless engineered enzyme assembly for enhanced methanol utilization
    • Price, J. V., Chen, L., Whitaker, W. B., Papoutsakis, E., and Chen, W. (2016) Scaffoldless engineered enzyme assembly for enhanced methanol utilization Proc. Natl. Acad. Sci. U. S. A. 113, 12691-12696 10.1073/pnas.1601797113
    • (2016) Proc. Natl. Acad. Sci. U. S. A. , vol.113 , pp. 12691-12696
    • Price, J.V.1    Chen, L.2    Whitaker, W.B.3    Papoutsakis, E.4    Chen, W.5
  • 44
    • 85006132386 scopus 로고    scopus 로고
    • Enhanced itaconic acid production by self-assembly of two biosynthetic enzymes in Escherichia coli
    • Yang, Z., Gao, X., Xie, H., Wang, F., Ren, Y., and Wei, D. (2017) Enhanced itaconic acid production by self-assembly of two biosynthetic enzymes in Escherichia coli Biotechnol. Bioeng. 114, 457-462 10.1002/bit.26081
    • (2017) Biotechnol. Bioeng. , vol.114 , pp. 457-462
    • Yang, Z.1    Gao, X.2    Xie, H.3    Wang, F.4    Ren, Y.5    Wei, D.6
  • 46
    • 84923516258 scopus 로고    scopus 로고
    • A chromosomally encoded T7 RNA polymerase-dependent gene expression system for Corynebacterium glutamicum: Construction and comparative evaluation at the single-cell level
    • Kortmann, M., Kuhl, V., Klaffl, S., and Bott, M. (2015) A chromosomally encoded T7 RNA polymerase-dependent gene expression system for Corynebacterium glutamicum: construction and comparative evaluation at the single-cell level Microb. Biotechnol. 8, 253-265 10.1111/1751-7915.12236
    • (2015) Microb. Biotechnol. , vol.8 , pp. 253-265
    • Kortmann, M.1    Kuhl, V.2    Klaffl, S.3    Bott, M.4
  • 47
    • 84884188636 scopus 로고    scopus 로고
    • Construction of a prophage-free variant of Corynebacterium glutamicum ATCC 13032 for use as a platform strain for basic research and industrial biotechnology
    • Baumgart, M., Unthan, S., Ruckert, C., Sivalingam, J., Grunberger, A., Kalinowski, J., Bott, M., Noack, S., and Frunzke, J. (2013) Construction of a prophage-free variant of Corynebacterium glutamicum ATCC 13032 for use as a platform strain for basic research and industrial biotechnology Appl. Environ. Microbiol. 79, 6006-6015 10.1128/AEM.01634-13
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 6006-6015
    • Baumgart, M.1    Unthan, S.2    Ruckert, C.3    Sivalingam, J.4    Grunberger, A.5    Kalinowski, J.6    Bott, M.7    Noack, S.8    Frunzke, J.9
  • 48
    • 0027164654 scopus 로고
    • Isoleucine synthesis in Corynebacterium glutamicum - Molecular analysis of the IlvB-IlvN-IlvC operon
    • Keilhauer, C., Eggeling, L., and Sahm, H. (1993) Isoleucine synthesis in Corynebacterium glutamicum-Molecular analysis of the IlvB-IlvN-IlvC operon J. Bacteriol. 175, 5595-5603 10.1128/jb.175.17.5595-5603.1993
    • (1993) J. Bacteriol. , vol.175 , pp. 5595-5603
    • Keilhauer, C.1    Eggeling, L.2    Sahm, H.3
  • 51
    • 0035041240 scopus 로고    scopus 로고
    • Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1
    • Niebisch, A. and Bott, M. (2001) Molecular analysis of the cytochrome bc1-aa3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c1 Arch. Microbiol. 175, 282-294 10.1007/s002030100262
    • (2001) Arch. Microbiol. , vol.175 , pp. 282-294
    • Niebisch, A.1    Bott, M.2
  • 52
    • 0021874595 scopus 로고
    • Purification of two alcohol dehydrogenases from Zymomonas mobilis and their properties
    • Kinoshita, S., Kakizono, T., Kadota, K., Das, K., and Taguchi, H. (1985) Purification of two alcohol dehydrogenases from Zymomonas mobilis and their properties Appl. Microbiol. Biotechnol. 22, 249-254 10.1007/BF00252025
    • (1985) Appl. Microbiol. Biotechnol. , vol.22 , pp. 249-254
    • Kinoshita, S.1    Kakizono, T.2    Kadota, K.3    Das, K.4    Taguchi, H.5
  • 53
    • 29244468900 scopus 로고    scopus 로고
    • Construction and expression of an ethanol production operon in Gram-positive bacteria
    • Talarico, L. A., Gil, M. A., Yomano, L. P., Ingram, L. O., and Maupin-Furlow, J. A. (2005) Construction and expression of an ethanol production operon in Gram-positive bacteria Microbiology 151, 4023-4031 10.1099/mic.0.28375-0
    • (2005) Microbiology , vol.151 , pp. 4023-4031
    • Talarico, L.A.1    Gil, M.A.2    Yomano, L.P.3    Ingram, L.O.4    Maupin-Furlow, J.A.5


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