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Volumn 130, Issue 6, 2021, Pages 1839-1856

Positioning Bacillus subtilis as terpenoid cell factory

Author keywords

Bacillus subtilis; cell factory; MEP pathway; metabolic engineering; terpenoids

Indexed keywords

BACTERIOLOGY; BIOCHEMISTRY; BIOSYNTHESIS; CELLS; CYTOLOGY; ISOPRENE; LIPIDS; METABOLISM;

EID: 85096707856     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/jam.14904     Document Type: Review
Times cited : (18)

References (123)
  • 1
    • 85049395876 scopus 로고    scopus 로고
    • Catalysis of amorpha-4,11-diene synthase unraveled and improved by mutability landscape guided engineering
    • Abdallah, I.I., van Merkerk, R., Klumpenaar, E. and Quax, W.J. (2018) Catalysis of amorpha-4,11-diene synthase unraveled and improved by mutability landscape guided engineering. Sci Rep 8, 9961.
    • (2018) Sci Rep , vol.8 , pp. 9961
    • Abdallah, I.I.1    van Merkerk, R.2    Klumpenaar, E.3    Quax, W.J.4
  • 2
    • 85077529686 scopus 로고    scopus 로고
    • A regulated synthetic operon facilitates stable overexpression of multigene terpenoid pathway in Bacillus subtilis
    • Abdallah, I.I., Xue, D., Pramastya, H., van Merkerk, R., Setroikromo, R. and Quax, W.J. (2020) A regulated synthetic operon facilitates stable overexpression of multigene terpenoid pathway in Bacillus subtilis. J Ind Microbiol Biotechnol 47, 243–249.
    • (2020) J Ind Microbiol Biotechnol , vol.47 , pp. 243-249
    • Abdallah, I.I.1    Xue, D.2    Pramastya, H.3    van Merkerk, R.4    Setroikromo, R.5    Quax, W.J.6
  • 3
    • 85065903593 scopus 로고    scopus 로고
    • Metabolic engineering of Bacillus subtilis toward taxadiene biosynthesis as the first committed step for taxol production
    • Abdallah, I.I., Pramastya, H., van Merkerk, R., Sukrasno, S. and Quax, W.J. (2019) Metabolic engineering of Bacillus subtilis toward taxadiene biosynthesis as the first committed step for taxol production. Front Microbiol 10, 218–227. http://doi.org/10.3389/fmicb.2019.00218
    • (2019) Front Microbiol , vol.10 , pp. 218-227
    • Abdallah, I.I.1    Pramastya, H.2    van Merkerk, R.3    Sukrasno, S.4    Quax, W.J.5
  • 5
    • 84862642945 scopus 로고    scopus 로고
    • Influence of oxidative and nitrosative stress on accumulation of diphosphate intermediates of the non-mevalonate pathway of isoprenoid biosynthesis in corynebacteria and mycobacteria
    • Artsatbanov, V.Y., Vostroknutova, G.N., Shleeva, M.O., Goncharenko, A.V., Zinin, A.I., Ostrovsky, D.N. and Kapreliants, A.S. (2012) Influence of oxidative and nitrosative stress on accumulation of diphosphate intermediates of the non-mevalonate pathway of isoprenoid biosynthesis in corynebacteria and mycobacteria. Biochemistry 77, 362–371.
    • (2012) Biochemistry , vol.77 , pp. 362-371
    • Artsatbanov, V.Y.1    Vostroknutova, G.N.2    Shleeva, M.O.3    Goncharenko, A.V.4    Zinin, A.I.5    Ostrovsky, D.N.6    Kapreliants, A.S.7
  • 6
    • 84937605477 scopus 로고    scopus 로고
    • Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli
    • Bakkes, P.J., Biemann, S., Bokel, A., Eickholt, M., Girhard, M. and Urlacher, V.B. (2015) Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli. Sci Rep 5, https://doi.org/10.1038/srep12158.
    • (2015) Sci Rep , vol.5
    • Bakkes, P.J.1    Biemann, S.2    Bokel, A.3    Eickholt, M.4    Girhard, M.5    Urlacher, V.B.6
  • 7
    • 84984663977 scopus 로고    scopus 로고
    • Engineering of recombinant poplar deoxy-D-xylulose-5-phosphate synthase (PtDXS) by site-directed mutagenesis improves its activity
    • Banerjee, A., Preiser, A.L. and Sharkey, T.D. (2016) Engineering of recombinant poplar deoxy-D-xylulose-5-phosphate synthase (PtDXS) by site-directed mutagenesis improves its activity. PLoS One 11, e0161534.
    • (2016) PLoS One , vol.11
    • Banerjee, A.1    Preiser, A.L.2    Sharkey, T.D.3
  • 8
    • 84904173300 scopus 로고    scopus 로고
    • Methylerythritol 4-phosphate (MEP) pathway metabolic regulation
    • Banerjee, A. and Sharkey, T.D. (2014) Methylerythritol 4-phosphate (MEP) pathway metabolic regulation. Nat Prod Rep 31, 1043–1055.
    • (2014) Nat Prod Rep , vol.31 , pp. 1043-1055
    • Banerjee, A.1    Sharkey, T.D.2
  • 9
    • 84878768243 scopus 로고    scopus 로고
    • Feedback Inhibition of deoxy-d-xylulose-5-phosphate synthase regulates the methylerythritol 4-phosphate pathway
    • Banerjee, A., Wu, Y., Banerjee, R., Li, Y., Yan, H. and Sharkey, T.D. (2013) Feedback Inhibition of deoxy-d-xylulose-5-phosphate synthase regulates the methylerythritol 4-phosphate pathway. J Biol Chem 288, 16926–16936.
    • (2013) J Biol Chem , vol.288 , pp. 16926-16936
    • Banerjee, A.1    Wu, Y.2    Banerjee, R.3    Li, Y.4    Yan, H.5    Sharkey, T.D.6
  • 10
    • 84948783764 scopus 로고    scopus 로고
    • Class I and class II lanthipeptides produced by Bacillus spp
    • Barbosa, J., Caetano, T. and Mendo, S. (2015) Class I and class II lanthipeptides produced by Bacillus spp. J Nat Prod 78, 2850–2866.
    • (2015) J Nat Prod , vol.78 , pp. 2850-2866
    • Barbosa, J.1    Caetano, T.2    Mendo, S.3
  • 11
    • 84962250132 scopus 로고    scopus 로고
    • Overcoming heterologous protein interdependency to optimize P450-mediated Taxol precursor synthesis in Escherichia coli
    • Biggs, B.W., Lim, C.G., Sagliani, K., Shankar, S., Stephanopoulos, G., De Mey, M. and Ajikumar, P.K. (2016) Overcoming heterologous protein interdependency to optimize P450-mediated Taxol precursor synthesis in Escherichia coli. Proc Natl Acad Sci 113, 3209–3214.
    • (2016) Proc Natl Acad Sci , vol.113 , pp. 3209-3214
    • Biggs, B.W.1    Lim, C.G.2    Sagliani, K.3    Shankar, S.4    Stephanopoulos, G.5    De Mey, M.6    Ajikumar, P.K.7
  • 12
    • 84867838237 scopus 로고    scopus 로고
    • 2 C-methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity
    • Bitok, J.K. and Meyers, C.F. (2012) 2 C-methyl-d-erythritol 4-phosphate enhances and sustains cyclodiphosphate synthase IspF activity. ACS Chem Biol 7, 1702–1710.
    • (2012) ACS Chem Biol , vol.7 , pp. 1702-1710
    • Bitok, J.K.1    Meyers, C.F.2
  • 13
    • 44349145919 scopus 로고    scopus 로고
    • A polycyclic terpenoid that alleviates oxidative stress
    • Bosak, T., Losick, R.M. and Pearson, A. (2008) A polycyclic terpenoid that alleviates oxidative stress. Proc Natl Acad Sci 105, 6725–6729.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 6725-6729
    • Bosak, T.1    Losick, R.M.2    Pearson, A.3
  • 15
    • 85013777700 scopus 로고    scopus 로고
    • A novel approach to improve poly-γ-glutamic acid production by NADPH regeneration in Bacillus licheniformis WX-02
    • Cai, D., He, P., Lu, X., Zhu, C., Zhu, J., Zhan, Y., Wang, Q., Wen, Z. et al. (2017) A novel approach to improve poly-γ-glutamic acid production by NADPH regeneration in Bacillus licheniformis WX-02. Sci Rep 7, 43404.
    • (2017) Sci Rep , vol.7 , pp. 43404
    • Cai, D.1    He, P.2    Lu, X.3    Zhu, C.4    Zhu, J.5    Zhan, Y.6    Wang, Q.7    Wen, Z.8
  • 16
    • 33745181160 scopus 로고    scopus 로고
    • Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis
    • Calderone, C.T., Kowtoniuk, W.E., Kelleher, N.L., Walsh, C.T. and Dorrestein, P.C. (2006) Convergence of isoprene and polyketide biosynthetic machinery: isoprenyl-S-carrier proteins in the pksX pathway of Bacillus subtilis. Proc Natl Acad Sci USA 103, 8977–8982.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8977-8982
    • Calderone, C.T.1    Kowtoniuk, W.E.2    Kelleher, N.L.3    Walsh, C.T.4    Dorrestein, P.C.5
  • 18
    • 85069489878 scopus 로고    scopus 로고
    • An engineered B. subtilis inducible promoter system with over 10,000-fold dynamic range
    • Castillo-Hair, S., Fujita, M., Igoshin, O.A. and Tabor, J.J. (2019) An engineered B. subtilis inducible promoter system with over 10,000-fold dynamic range. ACS Synth Biol acssynbio.8b00469.
    • (2019) ACS Synth Biol
    • Castillo-Hair, S.1    Fujita, M.2    Igoshin, O.A.3    Tabor, J.J.4
  • 19
    • 85065920609 scopus 로고    scopus 로고
    • Overview of the antimicrobial compounds produced by members of the Bacillus subtilis group
    • Caulier, S., Nannan, C., Gillis, A., Licciardi, F., Bragard, C. and Mahillon, J. (2019) Overview of the antimicrobial compounds produced by members of the Bacillus subtilis group. Front Microbiol 10, https://doi.org/10.3389/fmicb.2019.00302
    • (2019) Front Microbiol , vol.10
    • Caulier, S.1    Nannan, C.2    Gillis, A.3    Licciardi, F.4    Bragard, C.5    Mahillon, J.6
  • 20
    • 56549084929 scopus 로고    scopus 로고
    • Making artemisinin
    • Covello, P.S. (2008) Making artemisinin. Phytochemistry 69, 2881–2885.
    • (2008) Phytochemistry , vol.69 , pp. 2881-2885
    • Covello, P.S.1
  • 21
    • 85071354562 scopus 로고    scopus 로고
    • Engineering a bifunctional Phr60-Rap60-Spo0A quorum-sensing molecular switch for dynamic fine-tuning of menaquinone-7 synthesis in Bacillus subtilis
    • Cui, S., Lv, X., Wu, Y., Li, J., Du, G., Ledesma-Amaro, R. and Liu, L. (2019) Engineering a bifunctional Phr60-Rap60-Spo0A quorum-sensing molecular switch for dynamic fine-tuning of menaquinone-7 synthesis in Bacillus subtilis. ACS Synth Biol 8, 1826–1837.
    • (2019) ACS Synth Biol , vol.8 , pp. 1826-1837
    • Cui, S.1    Lv, X.2    Wu, Y.3    Li, J.4    Du, G.5    Ledesma-Amaro, R.6    Liu, L.7
  • 22
    • 0036005606 scopus 로고    scopus 로고
    • The biosynthesis of C5–C25 terpenoid compounds
    • Dewick, P.M. (2002) The biosynthesis of C5–C25 terpenoid compounds. Nat Prod Rep 19, 181–222.
    • (2002) Nat Prod Rep , vol.19 , pp. 181-222
    • Dewick, P.M.1
  • 24
    • 84901459476 scopus 로고    scopus 로고
    • Current development in genetic engineering strategies of Bacillus species
    • Dong, H. and Zhang, D. (2014) Current development in genetic engineering strategies of Bacillus species. Microb Cell Fact 13, 63.
    • (2014) Microb Cell Fact , vol.13 , pp. 63
    • Dong, H.1    Zhang, D.2
  • 25
    • 76849109846 scopus 로고    scopus 로고
    • Overexpression of glucose-6-phosphate dehydrogenase enhances riboflavin production in Bacillus subtilis
    • Duan, Y.X., Chen, T., Chen, X. and Zhao, X.M. (2010) Overexpression of glucose-6-phosphate dehydrogenase enhances riboflavin production in Bacillus subtilis. Appl Microbiol Biotechnol 85, 1907–1914.
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1907-1914
    • Duan, Y.X.1    Chen, T.2    Chen, X.3    Zhao, X.M.4
  • 27
    • 44749083814 scopus 로고    scopus 로고
    • Metabolic engineering of taxadiene biosynthesis in yeast as a first step towards Taxol (Paclitaxel) production
    • Engels, B., Dahm, P. and Jennewein, S. (2008) Metabolic engineering of taxadiene biosynthesis in yeast as a first step towards Taxol (Paclitaxel) production. Metab Eng 10, 201–206.
    • (2008) Metab Eng , vol.10 , pp. 201-206
    • Engels, B.1    Dahm, P.2    Jennewein, S.3
  • 28
    • 0034551758 scopus 로고    scopus 로고
    • Bacterial sources and sinks of isoprene, a reactive atmospheric hydrocarbon
    • Fall, R. and Copley, S.D. (2000) Bacterial sources and sinks of isoprene, a reactive atmospheric hydrocarbon. Environ Microbiol 2, 123–130.
    • (2000) Environ Microbiol , vol.2 , pp. 123-130
    • Fall, R.1    Copley, S.D.2
  • 29
    • 84911490656 scopus 로고    scopus 로고
    • Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production
    • Feng, X., Hu, Y., Zheng, Y., Zhu, W., Li, K., Huang, C.-H., Ko, T.-P., Ren, F. et al. (2014) Structural and functional analysis of Bacillus subtilis YisP reveals a role of its product in biofilm production. Chem Biol 21, 1557–1563.
    • (2014) Chem Biol , vol.21 , pp. 1557-1563
    • Feng, X.1    Hu, Y.2    Zheng, Y.3    Zhu, W.4    Li, K.5    Huang, C.-H.6    Ko, T.-P.7    Ren, F.8
  • 30
    • 84968831715 scopus 로고    scopus 로고
    • Two unexpected promiscuous activities of the iron–sulfur protein IspH in production of isoprene and isoamylene
    • Ge, D., Xue, Y. and Ma, Y. (2016) Two unexpected promiscuous activities of the iron–sulfur protein IspH in production of isoprene and isoamylene. Microb Cell Fact 15, 79.
    • (2016) Microb Cell Fact , vol.15 , pp. 79
    • Ge, D.1    Xue, Y.2    Ma, Y.3
  • 32
    • 68349152437 scopus 로고    scopus 로고
    • Regioselective biooxidation of (+)-valencene by recombinant E. coli expressing CYP109B1 from Bacillus subtilis in a two-liquid-phase system
    • Girhard, M., Machida, K., Itoh, M., Schmid, R.D., Arisawa, A. and Urlacher, V.B. (2009) Regioselective biooxidation of (+)-valencene by recombinant E. coli expressing CYP109B1 from Bacillus subtilis in a two-liquid-phase system. Microb Cell Fact 8, 36.
    • (2009) Microb Cell Fact , vol.8 , pp. 36
    • Girhard, M.1    Machida, K.2    Itoh, M.3    Schmid, R.D.4    Arisawa, A.5    Urlacher, V.B.6
  • 33
    • 85027052642 scopus 로고    scopus 로고
    • Boosting isoprene production via heterologous expression of the Kudzu isoprene synthase gene (kIspS) into Bacillus spp. cell factory
    • Gomaa, L., Loscar, M.E., Zein, H.S., Abdel-Ghaffar, N., Abdelhadi, A.A., Abdelaal, A.S. and Abdallah, N.A. (2017) Boosting isoprene production via heterologous expression of the Kudzu isoprene synthase gene (kIspS) into Bacillus spp. cell factory. AMB Express 7, https://doi.org/10.1186/s13568-017-0461-7
    • (2017) AMB Express , vol.7
    • Gomaa, L.1    Loscar, M.E.2    Zein, H.S.3    Abdel-Ghaffar, N.4    Abdelhadi, A.A.5    Abdelaal, A.S.6    Abdallah, N.A.7
  • 34
    • 0038529613 scopus 로고    scopus 로고
    • The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity
    • Grabowska, D. and Chelstowska, A. (2003) The ALD6 gene product is indispensable for providing NADPH in yeast cells lacking glucose-6-phosphate dehydrogenase activity. J Biol Chem 278, 13984–13988.
    • (2003) J Biol Chem , vol.278 , pp. 13984-13988
    • Grabowska, D.1    Chelstowska, A.2
  • 36
    • 85048835854 scopus 로고    scopus 로고
    • Advances and prospects of Bacillus subtilis cellular factories: from rational design to industrial applications
    • Gu, Y., Xu, X., Wu, Y., Niu, T., Liu, Y., Li, J., Du, G. and Liu, L. (2018) Advances and prospects of Bacillus subtilis cellular factories: from rational design to industrial applications. Metab Eng 50, 109–121.
    • (2018) Metab Eng , vol.50 , pp. 109-121
    • Gu, Y.1    Xu, X.2    Wu, Y.3    Niu, T.4    Liu, Y.5    Li, J.6    Du, G.7    Liu, L.8
  • 39
    • 2442552990 scopus 로고    scopus 로고
    • Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium
    • Gustafsson, M.C.U., Roitel, O., Marshall, K.R., Noble, M.A., Chapman, S.K., Pessegueiro, A., Fulco, A.J., Cheesman, M.R. et al. (2004) Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium. Biochemistry 43, 5474–5487.
    • (2004) Biochemistry , vol.43 , pp. 5474-5487
    • Gustafsson, M.C.U.1    Roitel, O.2    Marshall, K.R.3    Noble, M.A.4    Chapman, S.K.5    Pessegueiro, A.6    Fulco, A.J.7    Cheesman, M.R.8
  • 40
    • 0032811818 scopus 로고    scopus 로고
    • Escherichia coli open reading frame 696 is idi, a nonessential gene encoding isopentenyl diphosphate isomerase
    • Hahn, F.M., Hurlburt, A.P. and Poulter, C.D. (1999) Escherichia coli open reading frame 696 is idi, a nonessential gene encoding isopentenyl diphosphate isomerase. J Bacteriol 181, 4499–4504. https://doi.org/10.1128/JB.181.15.4499-4504.1999
    • (1999) J Bacteriol , vol.181 , pp. 4499-4504
    • Hahn, F.M.1    Hurlburt, A.P.2    Poulter, C.D.3
  • 41
    • 68049092197 scopus 로고    scopus 로고
    • Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction
    • Hazra, A., Chatterjee, A. and Begley, T.P. (2009) Biosynthesis of the thiamin thiazole in Bacillus subtilis: identification of the product of the thiazole synthase-catalyzed reaction. J Am Chem Soc 131, 3225–3229.
    • (2009) J Am Chem Soc , vol.131 , pp. 3225-3229
    • Hazra, A.1    Chatterjee, A.2    Begley, T.P.3
  • 42
    • 0036207004 scopus 로고    scopus 로고
    • Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme a reductase, a dual-function protein of isopentenyl diphosphate
    • Hedl, M., Sutherlin, A., Wilding, E.I., Mazzulla, M., Mcdevitt, D., Lane, P., Ii, J.W.B., Lehnbeuter, K.R. et al. (2002) Enterococcus faecalis acetoacetyl-coenzyme A thiolase/3-hydroxy-3-methylglutaryl-coenzyme a reductase, a dual-function protein of isopentenyl diphosphate. Biosynthesis 184, 2116–2122.
    • (2002) Biosynthesis , vol.184 , pp. 2116-2122
    • Hedl, M.1    Sutherlin, A.2    Wilding, E.I.3    Mazzulla, M.4    Mcdevitt, D.5    Lane, P.6    Ii, J.W.B.7    Lehnbeuter, K.R.8
  • 43
    • 84879232156 scopus 로고    scopus 로고
    • Coregulation of terpenoid pathway genes and prediction of isoprene production in Bacillus subtilis using transcriptomics
    • Hess, B.M., Xue, J., Markillie, L.M., Taylor, R.C., Wiley, H.S., Ahring, B.K. and Linggi, B. (2013) Coregulation of terpenoid pathway genes and prediction of isoprene production in Bacillus subtilis using transcriptomics. PLoS One 8, e66104.
    • (2013) PLoS One , vol.8
    • Hess, B.M.1    Xue, J.2    Markillie, L.M.3    Taylor, R.C.4    Wiley, H.S.5    Ahring, B.K.6    Linggi, B.7
  • 44
    • 84863678387 scopus 로고    scopus 로고
    • HmgR, a key enzyme in the mevalonate pathway for isoprenoid biosynthesis, is essential for growth of Listeria monocytogenes EGDe
    • Heuston, S., Begley, M., Davey, M.S., Eberl, M., Casey, P.G., Hill, C. and Gahan, C.G.M. (2012) HmgR, a key enzyme in the mevalonate pathway for isoprenoid biosynthesis, is essential for growth of Listeria monocytogenes EGDe. Microbiology 158, 1684–1693.
    • (2012) Microbiology , vol.158 , pp. 1684-1693
    • Heuston, S.1    Begley, M.2    Davey, M.S.3    Eberl, M.4    Casey, P.G.5    Hill, C.6    Gahan, C.G.M.7
  • 45
    • 33845184925 scopus 로고
    • Biosynthesis of vitamin B6: incorporation of D-1-deoxyxylulose
    • Hill, R.E., Sayer, B.G. and Spenser, I.D. (1989) Biosynthesis of vitamin B6: incorporation of D-1-deoxyxylulose. J Am Chem Soc 111, 1916–1917.
    • (1989) J Am Chem Soc , vol.111 , pp. 1916-1917
    • Hill, R.E.1    Sayer, B.G.2    Spenser, I.D.3
  • 46
  • 47
    • 34247131307 scopus 로고    scopus 로고
    • Enzyme promiscuity: mechanism and applications
    • Hult, K. and Berglund, P. (2007) Enzyme promiscuity: mechanism and applications. Trends Biotechnol 25, 231–238.
    • (2007) Trends Biotechnol , vol.25 , pp. 231-238
    • Hult, K.1    Berglund, P.2
  • 48
    • 84994469233 scopus 로고    scopus 로고
    • A structural and functional study on the 2-C-methyl-d-erythritol-4-phosphate cytidyltransferase (IspD) from Bacillus subtilis
    • Jin, Y., Liu, Z., Li, Y., Liu, W., Tao, Y. and Wang, G. (2016) A structural and functional study on the 2-C-methyl-d-erythritol-4-phosphate cytidyltransferase (IspD) from Bacillus subtilis. Sci Rep 6, 36379.
    • (2016) Sci Rep , vol.6 , pp. 36379
    • Jin, Y.1    Liu, Z.2    Li, Y.3    Liu, W.4    Tao, Y.5    Wang, G.6
  • 49
    • 34250828514 scopus 로고    scopus 로고
    • Functional analysis of genes involved in the biosynthesis of isoprene in Bacillus subtilis
    • Julsing, M.K., Rijpkema, M., Woerdenbag, H.J., Quax, W.J. and Kayser, O. (2007) Functional analysis of genes involved in the biosynthesis of isoprene in Bacillus subtilis. Appl Microbiol Biotechnol 75, 1377–1384.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1377-1384
    • Julsing, M.K.1    Rijpkema, M.2    Woerdenbag, H.J.3    Quax, W.J.4    Kayser, O.5
  • 51
    • 85055422864 scopus 로고    scopus 로고
    • Rerouting of NADPH synthetic pathways for increased protopanaxadiol production in Saccharomyces cerevisiae
    • Kim, J.-E., Jang, I.-S., Sung, B.H., Kim, S.C. and Lee, J.Y. (2018) Rerouting of NADPH synthetic pathways for increased protopanaxadiol production in Saccharomyces cerevisiae. Sci Rep 8, 15820.
    • (2018) Sci Rep , vol.8 , pp. 15820
    • Kim, J.-E.1    Jang, I.-S.2    Sung, B.H.3    Kim, S.C.4    Lee, J.Y.5
  • 52
    • 84903398330 scopus 로고    scopus 로고
    • Accumulation of heptaprenyl diphosphate sensitizes Bacillus subtilis to bacitracin: implications for the mechanism of resistance mediated by the BceAB transporter
    • Kingston, A.W., Zhao, H., Cook, G.M. and Helmann, J.D. (2014) Accumulation of heptaprenyl diphosphate sensitizes Bacillus subtilis to bacitracin: implications for the mechanism of resistance mediated by the BceAB transporter. Mol Microbiol 93, 37–49.
    • (2014) Mol Microbiol , vol.93 , pp. 37-49
    • Kingston, A.W.1    Zhao, H.2    Cook, G.M.3    Helmann, J.D.4
  • 54
    • 51549105375 scopus 로고    scopus 로고
    • The genes and enzymes involved in the biosynthesis of thiamin and thiamin diphosphate in yeasts
    • Kowalska, E. and Kozik, A. (2008) The genes and enzymes involved in the biosynthesis of thiamin and thiamin diphosphate in yeasts. Cell Mol Biol Lett 13, https://doi.org/10.2478/s11658-007-0055-5
    • (2008) Cell Mol Biol Lett , vol.13
    • Kowalska, E.1    Kozik, A.2
  • 55
    • 85006820162 scopus 로고    scopus 로고
    • Exploration of the 1-deoxy-d-xylulose 5-phosphate synthases suitable for the creation of a robust isoprenoid biosynthesis system
    • Kudoh, K., Kubota, G., Fujii, R., Kawano, Y. and Ihara, M. (2017) Exploration of the 1-deoxy-d-xylulose 5-phosphate synthases suitable for the creation of a robust isoprenoid biosynthesis system. J Biosci Bioeng 123, 300–307.
    • (2017) J Biosci Bioeng , vol.123 , pp. 300-307
    • Kudoh, K.1    Kubota, G.2    Fujii, R.3    Kawano, Y.4    Ihara, M.5
  • 57
    • 0037394552 scopus 로고    scopus 로고
    • Diversity of the biosynthesis of the isoprene units
    • Kuzuyama, T. and Seto, H. (2003) Diversity of the biosynthesis of the isoprene units. Nat Prod Rep 20, 171–183.
    • (2003) Nat Prod Rep , vol.20 , pp. 171-183
    • Kuzuyama, T.1    Seto, H.2
  • 58
    • 0034700150 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis: the evolution of two ancient and distinct pathways across genomes
    • Lange, B.M., Rujan, T., Martin, W. and Croteau, R. (2000) Isoprenoid biosynthesis: the evolution of two ancient and distinct pathways across genomes. Proc Natl Acad Sci 97, 13172–13177.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 13172-13177
    • Lange, B.M.1    Rujan, T.2    Martin, W.3    Croteau, R.4
  • 59
    • 3042767995 scopus 로고    scopus 로고
    • Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways
    • Laupitz, R., Hecht, S., Amslinger, S., Zepeck, F., Kaiser, J., Richter, G., Schramek, N., Steinbacher, S. et al. (2004) Biochemical characterization of Bacillus subtilis type II isopentenyl diphosphate isomerase, and phylogenetic distribution of isoprenoid biosynthesis pathways. Eur J Biochem 271, 2658–2669.
    • (2004) Eur J Biochem , vol.271 , pp. 2658-2669
    • Laupitz, R.1    Hecht, S.2    Amslinger, S.3    Zepeck, F.4    Kaiser, J.5    Richter, G.6    Schramek, N.7    Steinbacher, S.8
  • 60
    • 4744337841 scopus 로고    scopus 로고
    • Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 bioI
    • Lawson, R.J., Von Wachenfeldt, C., Haq, I., Perkins, J. and Munro, A.W. (2004) Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 bioI. Biochemistry 43, 12390–12409.
    • (2004) Biochemistry , vol.43 , pp. 12390-12409
    • Lawson, R.J.1    Von Wachenfeldt, C.2    Haq, I.3    Perkins, J.4    Munro, A.W.5
  • 61
    • 79953284572 scopus 로고    scopus 로고
    • Lantibiotics, class I bacteriocins from the genus Bacillus
    • Lee, H. and Kim, H.Y. (2011) Lantibiotics, class I bacteriocins from the genus Bacillus. J Microbiol Biotechnol 21, 229–235. https://doi.org/10.4014/jmb.1010.10017.
    • (2011) J Microbiol Biotechnol , vol.21 , pp. 229-235
    • Lee, H.1    Kim, H.Y.2
  • 63
    • 84874378034 scopus 로고    scopus 로고
    • Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli
    • Lee, W.-H., Kim, J.-W., Park, E.-H., Han, N.S., Kim, M.-D. and Seo, J.-H. (2013a) Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli. Appl Microbiol Biotechnol 97, 1561–1569.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 1561-1569
    • Lee, W.-H.1    Kim, J.-W.2    Park, E.-H.3    Han, N.S.4    Kim, M.-D.5    Seo, J.-H.6
  • 64
    • 84876674407 scopus 로고    scopus 로고
    • Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation
    • Lee, W.-H., Kim, M.-D., Jin, Y.-S. and Seo, J.-H. (2013b) Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation. Appl Microbiol Biotechnol 97, 2761–2772.
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 2761-2772
    • Lee, W.-H.1    Kim, M.-D.2    Jin, Y.-S.3    Seo, J.-H.4
  • 66
    • 85049857785 scopus 로고    scopus 로고
    • Metabolic engineering for the production of isoprene and isopentenol by Escherichia coli
    • Li, M., Nian, R., Xian, M. and Zhang, H. (2018) Metabolic engineering for the production of isoprene and isopentenol by Escherichia coli. Appl Microbiol Biotechnol 102, 7725–7738.
    • (2018) Appl Microbiol Biotechnol , vol.102 , pp. 7725-7738
    • Li, M.1    Nian, R.2    Xian, M.3    Zhang, H.4
  • 67
    • 85030129319 scopus 로고    scopus 로고
    • Production of a bioactive unnatural ginsenoside by metabolically engineered yeasts based on a new UDP-glycosyltransferase from Bacillus subtilis
    • Liang, H., Hu, Z., Zhang, T., Gong, T., Chen, J., Zhu, P., Li, Y. and Yang, J. (2017) Production of a bioactive unnatural ginsenoside by metabolically engineered yeasts based on a new UDP-glycosyltransferase from Bacillus subtilis. Metab Eng 44, 60–69.
    • (2017) Metab Eng , vol.44 , pp. 60-69
    • Liang, H.1    Hu, Z.2    Zhang, T.3    Gong, T.4    Chen, J.5    Zhu, P.6    Li, Y.7    Yang, J.8
  • 68
    • 84861912736 scopus 로고    scopus 로고
    • Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins
    • Liu, Y.-L., Guerra, F., Wang, K., Wang, W., Li, J., Huang, C., Zhu, W., Houlihan, K. et al. (2012) Structure, function and inhibition of the two- and three-domain 4Fe-4S IspG proteins. Proc Natl Acad Sci 109, 8558–8563.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 8558-8563
    • Liu, Y.-L.1    Guerra, F.2    Wang, K.3    Wang, W.4    Li, J.5    Huang, C.6    Zhu, W.7    Houlihan, K.8
  • 69
    • 85043266557 scopus 로고    scopus 로고
    • Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway
    • Liu, Z., Jin, Y., Liu, W., Tao, Y. and Wang, G. (2018) Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway. Biosci Rep 38, https://doi.org/10.1042/BSR20171370.
    • (2018) Biosci Rep , vol.38
    • Liu, Z.1    Jin, Y.2    Liu, W.3    Tao, Y.4    Wang, G.5
  • 70
    • 78650467548 scopus 로고    scopus 로고
    • Origins and early evolution of the mevalonate pathway of isoprenoid biosynthesis in the three domains of life
    • Lombard, J. and Moreira, D. (2011) Origins and early evolution of the mevalonate pathway of isoprenoid biosynthesis in the three domains of life. Mol Biol Evol 28, 87–99.
    • (2011) Mol Biol Evol , vol.28 , pp. 87-99
    • Lombard, J.1    Moreira, D.2
  • 71
    • 84952705872 scopus 로고    scopus 로고
    • The bioenergetic costs of a gene
    • Lynch, M. and Marinov, G.K. (2015) The bioenergetic costs of a gene. Proc Natl Acad Sci 112, 15690–15695.
    • (2015) Proc Natl Acad Sci , vol.112 , pp. 15690-15695
    • Lynch, M.1    Marinov, G.K.2
  • 74
    • 85057496980 scopus 로고    scopus 로고
    • Enhanced vitamin K (menaquinone-7) production by Bacillus subtilis natto in biofilm reactors by optimization of glucose-based medium
    • Mahdinia, E., Demirci, A. and Berenjian, A. (2018) Enhanced vitamin K (menaquinone-7) production by Bacillus subtilis natto in biofilm reactors by optimization of glucose-based medium. Curr Pharm Biotechnol 19, 917–924.
    • (2018) Curr Pharm Biotechnol , vol.19 , pp. 917-924
    • Mahdinia, E.1    Demirci, A.2    Berenjian, A.3
  • 75
    • 0038391517 scopus 로고    scopus 로고
    • Engineering a mevalonate pathway in Escherichia coli for production of terpenoids
    • Martin, V.J.J., Pitera, D.J., Withers, S.T., Newman, J.D. and Keasling, J.D. (2003) Engineering a mevalonate pathway in Escherichia coli for production of terpenoids. Nat Biotechnol 21, 796–802.
    • (2003) Nat Biotechnol , vol.21 , pp. 796-802
    • Martin, V.J.J.1    Pitera, D.J.2    Withers, S.T.3    Newman, J.D.4    Keasling, J.D.5
  • 76
    • 0035814339 scopus 로고    scopus 로고
    • The in vivo synthesis of plant sesquiterpenes by Escherichia coli
    • Martin, V.J.J., Yoshikuni, Y. and Keasling, J.D. (2001) The in vivo synthesis of plant sesquiterpenes by Escherichia coli. Biotechnol Bioeng 75, 497–503.
    • (2001) Biotechnol Bioeng , vol.75 , pp. 497-503
    • Martin, V.J.J.1    Yoshikuni, Y.2    Keasling, J.D.3
  • 77
    • 57049150799 scopus 로고    scopus 로고
    • Replacing Escherichia coli NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with a NADP-dependent enzyme from Clostridium acetobutylicum facilitates NADPH dependent pathways
    • Martínez, I., Zhu, J., Lin, H., Bennett, G.N. and San, K.-Y. (2008) Replacing Escherichia coli NAD-dependent glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with a NADP-dependent enzyme from Clostridium acetobutylicum facilitates NADPH dependent pathways. Metab Eng 10, 352–359.
    • (2008) Metab Eng , vol.10 , pp. 352-359
    • Martínez, I.1    Zhu, J.2    Lin, H.3    Bennett, G.N.4    San, K.-Y.5
  • 79
    • 0031905297 scopus 로고    scopus 로고
    • Rolling-circle plasmids from Bacillus subtilis: Complete nucleolide sequences and analyses of genes of pTA1015, pTA1040, pTA1050 and pTA1060, and comparisons with related plasmids from Gram-positive bacteria
    • Meijer, W.J.J., Wisman, G.B.A., Terpstra, P., Thorsted, P.B., Thomas, C.M., Holsappel, S., Venema, G. and Bron, S. (1998) Rolling-circle plasmids from Bacillus subtilis: Complete nucleolide sequences and analyses of genes of pTA1015, pTA1040, pTA1050 and pTA1060, and comparisons with related plasmids from Gram-positive bacteria. FEMS Microbiol Rev.
    • (1998) FEMS Microbiol Rev
    • Meijer, W.J.J.1    Wisman, G.B.A.2    Terpstra, P.3    Thorsted, P.B.4    Thomas, C.M.5    Holsappel, S.6    Venema, G.7    Bron, S.8
  • 80
    • 0032870941 scopus 로고    scopus 로고
    • Codon usage and lateral gene transfer in Bacillus subtilis
    • Moszer, I., Rocha, E.P. and Danchin, A. (1999) Codon usage and lateral gene transfer in Bacillus subtilis. Curr Opin Microbiol 2, 524–528.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 524-528
    • Moszer, I.1    Rocha, E.P.2    Danchin, A.3
  • 81
    • 27144523463 scopus 로고    scopus 로고
    • Construction of plasmid-based expression vectors for Bacillus subtilis exhibiting full structural stability
    • Nguyen, H.D., Nguyen, Q.A., Ferreira, R.C., Ferreira, L.C.S., Tran, L.T. and Schumann, W. (2005) Construction of plasmid-based expression vectors for Bacillus subtilis exhibiting full structural stability. Plasmid 54, 241–248.
    • (2005) Plasmid , vol.54 , pp. 241-248
    • Nguyen, H.D.1    Nguyen, Q.A.2    Ferreira, R.C.3    Ferreira, L.C.S.4    Tran, L.T.5    Schumann, W.6
  • 83
    • 84868531635 scopus 로고    scopus 로고
    • Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by glyceraldehyde-3-phosphate
    • Patel, H., Nemeria, N.S., Brammer, L.A., Freel Meyers, C.L. and Jordan, F. (2012) Observation of thiamin-bound intermediates and microscopic rate constants for their interconversion on 1-deoxy-xylulose 5-phosphate synthase: 600-fold rate acceleration of pyruvate decarboxylation by glyceraldehyde-3-phosphate. J Am Chem Soc 134, 18374–18379.
    • (2012) J Am Chem Soc , vol.134 , pp. 18374-18379
    • Patel, H.1    Nemeria, N.S.2    Brammer, L.A.3    Freel Meyers, C.L.4    Jordan, F.5
  • 84
    • 85033369527 scopus 로고    scopus 로고
    • The Bacillus BioBrick Box 2.0: expanding the genetic toolbox for the standardized work with Bacillus subtilis
    • Popp, P.F., Dotzler, M., Radeck, J., Bartels, J. and Mascher, T. (2017) The Bacillus BioBrick Box 2.0: expanding the genetic toolbox for the standardized work with Bacillus subtilis. Sci Rep 7, 15058.
    • (2017) Sci Rep , vol.7 , pp. 15058
    • Popp, P.F.1    Dotzler, M.2    Radeck, J.3    Bartels, J.4    Mascher, T.5
  • 85
    • 21244464767 scopus 로고    scopus 로고
    • fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis
    • Puan, K.J., Wang, H., Dairi, T., Kuzuyama, T. and Morita, C.T. (2005) fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis. FEBS Lett 579, 3802–3806.
    • (2005) FEBS Lett , vol.579 , pp. 3802-3806
    • Puan, K.J.1    Wang, H.2    Dairi, T.3    Kuzuyama, T.4    Morita, C.T.5
  • 86
    • 84888599866 scopus 로고    scopus 로고
    • The Bacillus BioBrick Box: generation and evaluation of essential genetic building blocks for standardized work with Bacillus subtilis
    • Radeck, J., Kraft, K., Bartels, J., Cikovic, T., Dürr, F., Emenegger, J., Kelterborn, S., Sauer, C. et al. (2013) The Bacillus BioBrick Box: generation and evaluation of essential genetic building blocks for standardized work with Bacillus subtilis. J Biol Eng 7, 29.
    • (2013) J Biol Eng , vol.7 , pp. 29
    • Radeck, J.1    Kraft, K.2    Bartels, J.3    Cikovic, T.4    Dürr, F.5    Emenegger, J.6    Kelterborn, S.7    Sauer, C.8
  • 87
    • 85083497851 scopus 로고    scopus 로고
    • Yeast metabolic engineering for the production of pharmaceutically important secondary metabolites
    • Rahmat, E. and Kang, Y. (2020) Yeast metabolic engineering for the production of pharmaceutically important secondary metabolites. Appl Microbiol Biotechnol 104, 4659–4674.
    • (2020) Appl Microbiol Biotechnol , vol.104 , pp. 4659-4674
    • Rahmat, E.1    Kang, Y.2
  • 88
    • 0034953307 scopus 로고    scopus 로고
    • Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis
    • Richard, S.B., Bowman, M.E., Kwiatkowski, W., Kang, I., Chow, C., Lillo, A.M., Cane, D.E. and Noel, J.P. (2001) Structure of 4-diphosphocytidyl-2-C-methylerythritol synthetase involved in mevalonate-independent isoprenoid biosynthesis. Nat Struct Biol 8, 641–648.
    • (2001) Nat Struct Biol , vol.8 , pp. 641-648
    • Richard, S.B.1    Bowman, M.E.2    Kwiatkowski, W.3    Kang, I.4    Chow, C.5    Lillo, A.M.6    Cane, D.E.7    Noel, J.P.8
  • 90
    • 1942538348 scopus 로고    scopus 로고
    • Developments in the use of Bacillus species for industrial production
    • Schallmey, M., Singh, A. and Ward, O.P. (2004) Developments in the use of Bacillus species for industrial production. Can J Microbiol 50, 1–17.
    • (2004) Can J Microbiol , vol.50 , pp. 1-17
    • Schallmey, M.1    Singh, A.2    Ward, O.P.3
  • 91
    • 85043787473 scopus 로고    scopus 로고
    • Microbial cell factories for the production of terpenoid flavor and fragrance compounds
    • Schempp, F.M., Drummond, L., Buchhaupt, M. and Schrader, J. (2018) Microbial cell factories for the production of terpenoid flavor and fragrance compounds. J Agric Food Chem 66, 2247–2258.
    • (2018) J Agric Food Chem , vol.66 , pp. 2247-2258
    • Schempp, F.M.1    Drummond, L.2    Buchhaupt, M.3    Schrader, J.4
  • 92
    • 4544261266 scopus 로고    scopus 로고
    • Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC
    • Seo, D., Kamino, K., Inoue, K. and Sakurai, H. (2004) Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC. Arch Microbiol 182, 80–89.
    • (2004) Arch Microbiol , vol.182 , pp. 80-89
    • Seo, D.1    Kamino, K.2    Inoue, K.3    Sakurai, H.4
  • 93
    • 0023652058 scopus 로고
    • Synonymous codon usage in Bacillus subtilis reflects both translational selection and mutational biases
    • Shields, D.C. and Sharp, P.M. (1987) Synonymous codon usage in Bacillus subtilis reflects both translational selection and mutational biases. Nucleic Acids Res.
    • (1987) Nucleic Acids Res
    • Shields, D.C.1    Sharp, P.M.2
  • 94
    • 84855278206 scopus 로고    scopus 로고
    • Evidence of isoprenoid precursor toxicity in Bacillus subtilis
    • Sivy, T.L., Fall, R. and Rosenstiel, T.N. (2011) Evidence of isoprenoid precursor toxicity in Bacillus subtilis. Biosci Biotechnol Biochem 75, 2376–2383.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 2376-2383
    • Sivy, T.L.1    Fall, R.2    Rosenstiel, T.N.3
  • 95
    • 0036295344 scopus 로고    scopus 로고
    • Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis
    • Sivy, T.L., Shirk, M.C. and Fall, R. (2002) Isoprene synthase activity parallels fluctuations of isoprene release during growth of Bacillus subtilis. Biochem Biophys Res Commun 294, 71–75.
    • (2002) Biochem Biophys Res Commun , vol.294 , pp. 71-75
    • Sivy, T.L.1    Shirk, M.C.2    Fall, R.3
  • 97
    • 84867010591 scopus 로고    scopus 로고
    • Discovery of acetylene hydratase activity of the iron-sulphur protein IspH
    • Span, I., Wang, K., Wang, W., Zhang, Y., Bacher, A., Eisenreich, W., Li, K., Schulz, C. et al. (2012) Discovery of acetylene hydratase activity of the iron-sulphur protein IspH. Nat Commun 3, https://doi.org/10.1038/ncomms2052.
    • (2012) Nat Commun , vol.3
    • Span, I.1    Wang, K.2    Wang, W.3    Zhang, Y.4    Bacher, A.5    Eisenreich, W.6    Li, K.7    Schulz, C.8
  • 98
    • 0037868855 scopus 로고    scopus 로고
    • Crystal structure of the type II isopentenyl diphosphate: dimethylallyl diphosphate isomerase fromBacillus subtilis
    • Steinbacher, S., Kaiser, J., Gerhardt, S., Eisenreich, W., Huber, R., Bacher, A. and Rohdich, F. (2003) Crystal structure of the type II isopentenyl diphosphate: dimethylallyl diphosphate isomerase fromBacillus subtilis. J Mol Biol 329, 973–982.
    • (2003) J Mol Biol , vol.329 , pp. 973-982
    • Steinbacher, S.1    Kaiser, J.2    Gerhardt, S.3    Eisenreich, W.4    Huber, R.5    Bacher, A.6    Rohdich, F.7
  • 99
    • 85060003685 scopus 로고    scopus 로고
    • New CRISPR-Cas9 vectors for genetic modifications of Bacillus species
    • Toymentseva, A.A. and Altenbuchner, J. (2019) New CRISPR-Cas9 vectors for genetic modifications of Bacillus species. FEMS Microbiol Lett 366.
    • (2019) FEMS Microbiol Lett , vol.366
    • Toymentseva, A.A.1    Altenbuchner, J.2
  • 100
    • 84879142653 scopus 로고    scopus 로고
    • High-level production of amorpha-4, 11-diene, a precursor of the antimalarial agent artemisinin, in Escherichia coli
    • Tsuruta, H., Paddon, C.J., Eng, D., Lenihan, J.R., Horning, T., Anthony, L.C., Regentin, R., Keasling, J.D. et al. (2009) High-level production of amorpha-4, 11-diene, a precursor of the antimalarial agent artemisinin, in Escherichia coli. PLoS One 4, e4489.
    • (2009) PLoS One , vol.4
    • Tsuruta, H.1    Paddon, C.J.2    Eng, D.3    Lenihan, J.R.4    Horning, T.5    Anthony, L.C.6    Regentin, R.7    Keasling, J.D.8
  • 101
    • 78649866559 scopus 로고    scopus 로고
    • Comparison of different Bacillus subtilis expression systems
    • Vavrová, Ľ., Muchová, K. and Barák, I. (2010) Comparison of different Bacillus subtilis expression systems. Res Microbiol 161, 791–797.
    • (2010) Res Microbiol , vol.161 , pp. 791-797
    • Vavrová, Ľ.1    Muchová, K.2    Barák, I.3
  • 102
    • 85074614631 scopus 로고    scopus 로고
    • Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis
    • Volke, D.C., Rohwer, J., Fischer, R. and Jennewein, S. (2019) Investigation of the methylerythritol 4-phosphate pathway for microbial terpenoid production through metabolic control analysis. Microb Cell Fact 18, 192.
    • (2019) Microb Cell Fact , vol.18 , pp. 192
    • Volke, D.C.1    Rohwer, J.2    Fischer, R.3    Jennewein, S.4
  • 103
    • 0033966887 scopus 로고    scopus 로고
    • Isoprene biosynthesis in Bacillus subtilis via the methylerythritol phosphate pathway
    • Wagner, W.P., Helmig, D. and Fall, R. (2000) Isoprene biosynthesis in Bacillus subtilis via the methylerythritol phosphate pathway. J Nat Prod 63, 37–40.
    • (2000) J Nat Prod , vol.63 , pp. 37-40
    • Wagner, W.P.1    Helmig, D.2    Fall, R.3
  • 104
    • 84892831820 scopus 로고    scopus 로고
    • Improvement of NADPH bioavailability in Escherichia coli by replacing NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase GapA with NADP (+)-dependent GapB from Bacillus subtilis and addition of NAD kinase
    • Wang, Y., San, K.-Y. and Bennett, G.N. (2013) Improvement of NADPH bioavailability in Escherichia coli by replacing NAD(+)-dependent glyceraldehyde-3-phosphate dehydrogenase GapA with NADP (+)-dependent GapB from Bacillus subtilis and addition of NAD kinase. J Ind Microbiol Biotechnol 40, 1449–1460.
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 1449-1460
    • Wang, Y.1    San, K.-Y.2    Bennett, G.N.3
  • 105
    • 84863187862 scopus 로고    scopus 로고
    • Bacillus subtilis genome editing using ssDNA with short homology regions
    • Wang, Y., Weng, J., Waseem, R., Yin, X., Zhang, R. and Shen, Q. (2012) Bacillus subtilis genome editing using ssDNA with short homology regions. Nucleic Acids Res 40, e91.
    • (2012) Nucleic Acids Res , vol.40
    • Wang, Y.1    Weng, J.2    Waseem, R.3    Yin, X.4    Zhang, R.5    Shen, Q.6
  • 106
    • 78651516949 scopus 로고    scopus 로고
    • Enhancement of riboflavin production with Bacillus subtilis by expression and site-directed mutagenesis of zwf and gnd gene from Corynebacterium glutamicum
    • Wang, Z., Chen, T., Ma, X., Shen, Z. and Zhao, X. (2011) Enhancement of riboflavin production with Bacillus subtilis by expression and site-directed mutagenesis of zwf and gnd gene from Corynebacterium glutamicum. Bioresour Technol 102, 3934–3940.
    • (2011) Bioresour Technol , vol.102 , pp. 3934-3940
    • Wang, Z.1    Chen, T.2    Ma, X.3    Shen, Z.4    Zhao, X.5
  • 107
    • 84855952259 scopus 로고    scopus 로고
    • P450 BM3 (CYP102A1): connecting the dots
    • Whitehouse, C.J.C., Bell, S.G. and Wong, L.-L. (2012) P450 BM3 (CYP102A1): connecting the dots. Chem Soc Rev 41, 1218–1260.
    • (2012) Chem Soc Rev , vol.41 , pp. 1218-1260
    • Whitehouse, C.J.C.1    Bell, S.G.2    Wong, L.-L.3
  • 108
    • 18544403253 scopus 로고    scopus 로고
    • Identification, evolution, and essentiality of the mevalonate pathway for isopentenyl diphosphate biosynthesis in gram-positive cocci
    • Wilding, E.I., Brown, J.R., Bryant, A.P., Chalker, A.F., Holmes, D.J., Ingraham, K.A., Iordanescu, S., So, C.Y. et al. (2000) Identification, evolution, and essentiality of the mevalonate pathway for isopentenyl diphosphate biosynthesis in gram-positive cocci. J Bacteriol 182, 4319–4327.
    • (2000) J Bacteriol , vol.182 , pp. 4319-4327
    • Wilding, E.I.1    Brown, J.R.2    Bryant, A.P.3    Chalker, A.F.4    Holmes, D.J.5    Ingraham, K.A.6    Iordanescu, S.7    So, C.Y.8
  • 109
    • 35148889024 scopus 로고    scopus 로고
    • Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity
    • Withers, S.T., Gottlieb, S.S., Lieu, B., Newman, J.D. and Keasling, J.D. (2007) Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity. Appl Environ Microbiol 73, 6277–6283.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 6277-6283
    • Withers, S.T.1    Gottlieb, S.S.2    Lieu, B.3    Newman, J.D.4    Keasling, J.D.5
  • 110
    • 0037464490 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein
    • Wolff, M., Seemann, M., Bui, B., Frapart, Y., Tritsch, D., Estrabot, A.G., Rodrı́guez-Concepción, M. (2003) Isoprenoid biosynthesis via the methylerythritol phosphate pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase (LytB/IspH) from Escherichia coli is a [4Fe-4S] protein. FEBS Lett 541, 115–120.
    • (2003) FEBS Lett , vol.541 , pp. 115-120
    • Wolff, M.1    Seemann, M.2    Bui, B.3    Frapart, Y.4    Tritsch, D.5    Estrabot, A.G.6    Rodrı́guez-Concepción, M.7
  • 111
    • 34047252866 scopus 로고    scopus 로고
    • Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis
    • Xiang, S., Usunow, G., Lange, G., Busch, M. and Tong, L. (2007) Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis. J Biol Chem.
    • (2007) J Biol Chem
    • Xiang, S.1    Usunow, G.2    Lange, G.3    Busch, M.4    Tong, L.5
  • 112
    • 84932192762 scopus 로고    scopus 로고
    • Enhanced C30carotenoid production in Bacillus subtilis by systematic overexpression of MEP pathway genes
    • Xue, D., Abdallah, I.I., de Haan, I.E.M., Sibbald, M.J.J.B. and Quax, W.J. (2015) Enhanced C30carotenoid production in Bacillus subtilis by systematic overexpression of MEP pathway genes. Appl Microbiol Biotechnol 99, 5907–5915.
    • (2015) Appl Microbiol Biotechnol , vol.99 , pp. 5907-5915
    • Xue, D.1    Abdallah, I.I.2    de Haan, I.E.M.3    Sibbald, M.J.J.B.4    Quax, W.J.5
  • 113
    • 79953268907 scopus 로고    scopus 로고
    • Enhancing isoprene production by genetic modification of the 1-deoxy-D-Xylulose-5-phosphate pathway in Bacillus subtilis
    • Xue, J. and Ahring, B.K. (2011) Enhancing isoprene production by genetic modification of the 1-deoxy-D-Xylulose-5-phosphate pathway in Bacillus subtilis. Appl Environ Microbiol 77, 2399–2405.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 2399-2405
    • Xue, J.1    Ahring, B.K.2
  • 114
    • 85077559158 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli for natural product biosynthesis
    • Yang, D., Park, S.Y., Park, Y.S., Eun, H. and Lee, S.Y. (2020) Metabolic engineering of Escherichia coli for natural product biosynthesis. Trends Biotechnol 38, 745–765.
    • (2020) Trends Biotechnol , vol.38 , pp. 745-765
    • Yang, D.1    Park, S.Y.2    Park, Y.S.3    Eun, H.4    Lee, S.Y.5
  • 115
    • 85060135976 scopus 로고    scopus 로고
    • Modular pathway engineering of Bacillus subtilis to promote de novo biosynthesis of menaquinone-7
    • Yang, S., Cao, Y., Sun, L., Li, C., Lin, X., Cai, Z., Zhang, G. and Song, H. (2019) Modular pathway engineering of Bacillus subtilis to promote de novo biosynthesis of menaquinone-7. ACS Synth Biol 8, 70–81.
    • (2019) ACS Synth Biol , vol.8 , pp. 70-81
    • Yang, S.1    Cao, Y.2    Sun, L.3    Li, C.4    Lin, X.5    Cai, Z.6    Zhang, G.7    Song, H.8
  • 116
    • 84955108367 scopus 로고    scopus 로고
    • Construction of a novel, stable, food-grade expression system by engineering the endogenous toxin-antitoxin system in Bacillus subtilis
    • Yang, S., Kang, Z., Cao, W., Du, G. and Chen, J. (2016) Construction of a novel, stable, food-grade expression system by engineering the endogenous toxin-antitoxin system in Bacillus subtilis. J Biotechnol 219, 40–47.
    • (2016) J Biotechnol , vol.219 , pp. 40-47
    • Yang, S.1    Kang, Z.2    Cao, W.3    Du, G.4    Chen, J.5
  • 117
    • 70350261481 scopus 로고    scopus 로고
    • Carotenoid production in Bacillus subtilis achieved by metabolic engineering
    • Yoshida, K., Ueda, S. and Maeda, I. (2009) Carotenoid production in Bacillus subtilis achieved by metabolic engineering. Biotechnol Lett 31, 1789–1793.
    • (2009) Biotechnol Lett , vol.31 , pp. 1789-1793
    • Yoshida, K.1    Ueda, S.2    Maeda, I.3
  • 118
    • 84991246572 scopus 로고    scopus 로고
    • Depletion of undecaprenyl pyrophosphate phosphatases disrupts cell envelope biogenesis in Bacillus subtilis
    • Zhao, H., Sun, Y., Peters, J.M., Gross, C.A., Garner, E.C. and Helmann, J.D. (2016) Depletion of undecaprenyl pyrophosphate phosphatases disrupts cell envelope biogenesis in Bacillus subtilis. J Bacteriol 198, 2925–2935.
    • (2016) J Bacteriol , vol.198 , pp. 2925-2935
    • Zhao, H.1    Sun, Y.2    Peters, J.M.3    Gross, C.A.4    Garner, E.C.5    Helmann, J.D.6
  • 119
    • 84875670791 scopus 로고    scopus 로고
    • Engineering central metabolic modules of Escherichia coli for improving β-carotene production
    • Zhao, J., Li, Q., Sun, T., Zhu, X., Xu, H., Tang, J., Zhang, X. and Ma, Y. (2013) Engineering central metabolic modules of Escherichia coli for improving β-carotene production. Metab Eng 17, 42–50.
    • (2013) Metab Eng , vol.17 , pp. 42-50
    • Zhao, J.1    Li, Q.2    Sun, T.3    Zhu, X.4    Xu, H.5    Tang, J.6    Zhang, X.7    Ma, Y.8
  • 120
    • 84941874386 scopus 로고    scopus 로고
    • Overexpression of ZWF1 and POS5 improves carotenoid biosynthesis in recombinant Saccharomyces cerevisiae
    • Zhao, X., Shi, F. and Zhan, W. (2015) Overexpression of ZWF1 and POS5 improves carotenoid biosynthesis in recombinant Saccharomyces cerevisiae. Lett Appl Microbiol 61, 354–360.
    • (2015) Lett Appl Microbiol , vol.61 , pp. 354-360
    • Zhao, X.1    Shi, F.2    Zhan, W.3
  • 121
    • 79958232375 scopus 로고    scopus 로고
    • Biosynthesis of isoprene in Escherichia coli via methylerythritol phosphate (MEP) pathway
    • Zhao, Y., Yang, J., Qin, B., Li, Y., Sun, Y., Su, S. and Xian, M. (2011) Biosynthesis of isoprene in Escherichia coli via methylerythritol phosphate (MEP) pathway. Appl Microbiol Biotechnol 90, 1915–1922.
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 1915-1922
    • Zhao, Y.1    Yang, J.2    Qin, B.3    Li, Y.4    Sun, Y.5    Su, S.6    Xian, M.7
  • 122
    • 84880792849 scopus 로고    scopus 로고
    • Optimization of amorphadiene synthesis in Bacillus subtilis via transcriptional, translational, and media modulation
    • Zhou, K., Zou, R., Zhang, C., Stephanopoulos, G. and Too, H.-P. (2013) Optimization of amorphadiene synthesis in Bacillus subtilis via transcriptional, translational, and media modulation. Biotechnol Bioeng 110, 2556–2561.
    • (2013) Biotechnol Bioeng , vol.110 , pp. 2556-2561
    • Zhou, K.1    Zou, R.2    Zhang, C.3    Stephanopoulos, G.4    Too, H.-P.5
  • 123
    • 85054291119 scopus 로고    scopus 로고
    • Enhancement of bacitracin production by NADPH generation via overexpressing glucose-6-phosphate dehydrogenase Zwf in Bacillus licheniformis
    • Zhu, S., Cai, D., Liu, Z., Zhang, B., Li, J., Chen, S. and Ma, X. (2019) Enhancement of bacitracin production by NADPH generation via overexpressing glucose-6-phosphate dehydrogenase Zwf in Bacillus licheniformis. Appl Biochem Biotechnol 187, 1502–1514.
    • (2019) Appl Biochem Biotechnol , vol.187 , pp. 1502-1514
    • Zhu, S.1    Cai, D.2    Liu, Z.3    Zhang, B.4    Li, J.5    Chen, S.6    Ma, X.7


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