메뉴 건너뛰기




Volumn 64, Issue , 2012, Pages 261-281

Molecular mechanisms and metabolic engineering of glutamate overproduction in corynebacterium glutamicum

Author keywords

2 Oxoglutarate dehydrogenase complex; Anaplerotic pathways; Corynebacterium glutamicum; Glutamate; Metabolic engineering; NCgl1221; OdhI

Indexed keywords

2 OXOGLUTARIC ACID; ALPHA-KETOGLUTARIC ACID; GLUTAMIC ACID; METHYLMALONYL COENZYME A DECARBOXYLASE;

EID: 84907227592     PISSN: 03060225     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-5055-5_13     Document Type: Article
Times cited : (16)

References (77)
  • 1
    • 33847207787 scopus 로고    scopus 로고
    • Altered metabolicflux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum
    • Asakura Y, Kimura E, Usuda Y, Kawahara Y, Matsui K, Osumi T, Nakamatsu T (2007) Altered metabolicflux due to deletion of odhA causes L-glutamate overproduction in Corynebacterium glutamicum. Appl Environ Microbiol 73: 1308-1319.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1308-1319
    • Asakura, Y.1    Kimura, E.2    Usuda, Y.3    Kawahara, Y.4    Matsui, K.5    Osumi, T.6    Nakamatsu, T.7
  • 2
    • 64049090659 scopus 로고    scopus 로고
    • Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism
    • Barthe P, Roumestand C, Canova MJ, Kremer L, Hurard C, Molle V, Cohen-Gonsaud M (2009) Dynamic and structural characterization of a bacterial FHA protein reveals a new autoinhibition mechanism. Structure 17: 568-578.
    • (2009) Structure , vol.17 , pp. 568-578
    • Barthe, P.1    Roumestand, C.2    Canova, M.J.3    Kremer, L.4    Hurard, C.5    Molle, V.6    Cohen-Gonsaud, M.7
  • 3
    • 84864801619 scopus 로고    scopus 로고
    • Systems and synthetic metabolic engineering for amino acid production-the heartbeat of industrial strain development
    • Becker J, Wittmann C (2012) Systems and synthetic metabolic engineering for amino acid production-the heartbeat of industrial strain development. Curr Opin Biotechnol. doi: 10. 1016/j. copbio. 2011. 1012. 1025.
    • (2012) Curr Opin Biotechnol
    • Becker, J.1    Wittmann, C.2
  • 4
    • 0026525773 scopus 로고
    • Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch-activated channels in bacteria
    • Berrier C, Coulombe A, Szabo I, Zoratti M, Ghazi A (1992) Gadolinium ion inhibits loss of metabolites induced by osmotic shock and large stretch-activated channels in bacteria. Eur J Biochem 206: 559-565.
    • (1992) Eur J Biochem , vol.206 , pp. 559-565
    • Berrier, C.1    Coulombe, A.2    Szabo, I.3    Zoratti, M.4    Ghazi, A.5
  • 5
    • 0026564643 scopus 로고
    • Molecular analysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase
    • Börmann ER, Eikmanns BJ, Sahm H (1992) Molecular analysis of the Corynebacterium glutamicum gdh gene encoding glutamate dehydrogenase. Mol Microbiol 6: 317-326.
    • (1992) Mol Microbiol , vol.6 , pp. 317-326
    • Börmann, E.R.1    Eikmanns, B.J.2    Sahm, H.3
  • 6
    • 78650640720 scopus 로고    scopus 로고
    • The properties and contribution of the Corynebacterium glutamicum MscS variant tofine-tuning of osmotic adaptation
    • Börngen K, Battle AR, Moker N, Morbach S, Marin K, Martinac B, Kramer R (2010) The properties and contribution of the Corynebacterium glutamicum MscS variant tofine-tuning of osmotic adaptation. Biochim Biophys Acta 1798: 2141-2149.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 2141-2149
    • Börngen, K.1    Battle, A.R.2    Moker, N.3    Morbach, S.4    Marin, K.5    Martinac, B.6    Kramer, R.7
  • 8
    • 0034625143 scopus 로고    scopus 로고
    • The Escherichia coli MG1655 in silico metabolic genotype: Its definition, characteristics, and capabilities
    • Edwards JS, Palsson BO (2000) The Escherichia coli MG1655 in silico metabolic genotype: its definition, characteristics, and capabilities. Proc Natl Acad Sci U S A 97: 5528-5533.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5528-5533
    • Edwards, J.S.1    Palsson, B.O.2
  • 9
    • 0035125986 scopus 로고    scopus 로고
    • In silico predictions of Escherichia coli metabolic capabilities are consistent with experimental data
    • Edwards JS, Ibarra RU, Palsson BO (2001) In silico predictions of Escherichia coli metabolic capabilities are consistent with experimental data. Nat Biotechnol 19: 125-130.
    • (2001) Nat Biotechnol , vol.19 , pp. 125-130
    • Edwards, J.S.1    Ibarra, R.U.2    Palsson, B.O.3
  • 10
    • 0028942304 scopus 로고
    • Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme
    • Eikmanns BJ, Rittmann D, Sahm H (1995) Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme. J Bacteriol 177: 774-782.
    • (1995) J Bacteriol , vol.177 , pp. 774-782
    • Eikmanns, B.J.1    Rittmann, D.2    Sahm, H.3
  • 12
    • 82355173361 scopus 로고    scopus 로고
    • Amino acid production from rice straw and wheat bran hydrolysates by recombinant pentose-utilizing Corynebacterium glutamicum
    • Gopinath V, Meiswinkel TM, Wendisch VF, Nampoothiri KM (2011) Amino acid production from rice straw and wheat bran hydrolysates by recombinant pentose-utilizing Corynebacterium glutamicum. Appl Microbiol Biotechnol 92: 985-996.
    • (2011) Appl Microbiol Biotechnol , vol.92 , pp. 985-996
    • Gopinath, V.1    Meiswinkel, T.M.2    Wendisch, V.F.3    Nampoothiri, K.M.4
  • 13
    • 39449104902 scopus 로고    scopus 로고
    • Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum
    • Hasegawa T, Hashimoto K, Kawasaki H, Nakamatsu T (2008) Changes in enzyme activities at the pyruvate node in glutamate-overproducing Corynebacterium glutamicum. J Biosci Bioeng 105: 12-19.
    • (2008) J Biosci Bioeng , vol.105 , pp. 12-19
    • Hasegawa, T.1    Hashimoto, K.2    Kawasaki, H.3    Nakamatsu, T.4
  • 15
  • 16
    • 0034102455 scopus 로고    scopus 로고
    • A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and L-glutamate production
    • Hirasawa T, Wachi M, Nagai K (2000) A mutation in the Corynebacterium glutamicum ltsA gene causes susceptibility to lysozyme, temperature-sensitive growth, and L-glutamate production. J Bacteriol 182: 2696-2701.
    • (2000) J Bacteriol , vol.182 , pp. 2696-2701
    • Hirasawa, T.1    Wachi, M.2    Nagai, K.3
  • 17
    • 0642280880 scopus 로고    scopus 로고
    • L-Glutamate production by lysozyme-sensitive Corynebacterium glutamicum ltsA mutant strains
    • Hirasawa T, Wachi M, Nagai K (2001) L-Glutamate production by lysozyme-sensitive Corynebacterium glutamicum ltsA mutant strains. BMC Biotechnol 1: 9.
    • (2001) BMC Biotechnol , vol.1
    • Hirasawa, T.1    Wachi, M.2    Nagai, K.3
  • 18
    • 0025300483 scopus 로고
    • Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum
    • Hoischen C, Kramer R (1990) Membrane alteration is necessary but not sufficient for effective glutamate secretion in Corynebacterium glutamicum. J Bacteriol 172: 3409-3416.
    • (1990) J Bacteriol , vol.172 , pp. 3409-3416
    • Hoischen, C.1    Kramer, R.2
  • 19
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: Features and impacts on biotechnological processes
    • Ikeda M, Nakagawa S (2003) The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl Microbiol Biotechnol 62: 99-109.
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 21
    • 33645890573 scopus 로고    scopus 로고
    • Gene expression of Corynebacterium glutamicum in response to the conditions inducing glutamate overproduction
    • Kataoka M, Hashimoto KI, Yoshida M, Nakamatsu T, Horinouchi S, Kawasaki H (2006) Gene expression of Corynebacterium glutamicum in response to the conditions inducing glutamate overproduction. Lett Appl Microbiol 42: 471-476.
    • (2006) Lett Appl Microbiol , vol.42 , pp. 471-476
    • Kataoka, M.1    Hashimoto, K.I.2    Yoshida, M.3    Nakamatsu, T.4    Horinouchi, S.5    Kawasaki, H.6
  • 24
    • 0031178552 scopus 로고    scopus 로고
    • Relationship between the glutamate production and the activity of 2-oxoglutarate dehydrogenase in Brevibacterium lactofermentum
    • Kawahara Y, Takahashi-Fuke K, Shimizu E, Nakamatsu T, Nakamori S (1997) Relationship between the glutamate production and the activity of 2-oxoglutarate dehydrogenase in Brevibacterium lactofermentum. Biosci Biotechnol Biochem 61: 1109-1112.
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1109-1112
    • Kawahara, Y.1    Takahashi-Fuke, K.2    Shimizu, E.3    Nakamatsu, T.4    Nakamori, S.5
  • 25
    • 0037229834 scopus 로고    scopus 로고
    • Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: Processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus
    • Kikuchi Y, Date M, Yokoyama K, Umezawa Y, Matsui H (2003) Secretion of active-form Streptoverticillium mobaraense transglutaminase by Corynebacterium glutamicum: processing of the pro-transglutaminase by a cosecreted subtilisin-like protease from Streptomyces albogriseolus. Appl Environ Microbiol 69: 358-366.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 358-366
    • Kikuchi, Y.1    Date, M.2    Yokoyama, K.3    Umezawa, Y.4    Matsui, H.5
  • 26
    • 58149165063 scopus 로고    scopus 로고
    • Effect of odhA overexpression and odhA antisense RNA expression on Tween-40-triggered glutamate production by Corynebacterium glutamicum
    • Kim J, Hirasawa T, Sato Y, Nagahisa K, Furusawa C, Shimizu H (2009) Effect of odhA overexpression and odhA antisense RNA expression on Tween-40-triggered glutamate production by Corynebacterium glutamicum. Appl Microbiol Biotechnol 81: 1097-1106.
    • (2009) Appl Microbiol Biotechnol , vol.81 , pp. 1097-1106
    • Kim, J.1    Hirasawa, T.2    Sato, Y.3    Nagahisa, K.4    Furusawa, C.5    Shimizu, H.6
  • 27
    • 77950629342 scopus 로고    scopus 로고
    • Requirement of de novo synthesis of the OdhI protein in penicillin-induced glutamate production by Corynebacterium glutamicum
    • Kim J, Fukuda H, Hirasawa T, Nagahisa K, Nagai K, Wachi M, Shimizu H (2010) Requirement of de novo synthesis of the OdhI protein in penicillin-induced glutamate production by Corynebacterium glutamicum. Appl Microbiol Biotechnol 86: 911-920.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 911-920
    • Kim, J.1    Fukuda, H.2    Hirasawa, T.3    Nagahisa, K.4    Nagai, K.5    Wachi, M.6    Shimizu, H.7
  • 28
    • 85027939622 scopus 로고    scopus 로고
    • Investigation of phosphorylation status of OdhI protein during penicillin-and Tween 40-triggered glutamate overproduction by Corynebacterium glutamicum
    • Kim J, Hirasawa T, Saito M, Furusawa C, Shimizu H (2011) Investigation of phosphorylation status of OdhI protein during penicillin-and Tween 40-triggered glutamate overproduction by Corynebacterium glutamicum. Appl Microbiol Biotechnol 91: 143-151.
    • (2011) Appl Microbiol Biotechnol , vol.91 , pp. 143-151
    • Kim, J.1    Hirasawa, T.2    Saito, M.3    Furusawa, C.4    Shimizu, H.5
  • 29
    • 0030266220 scopus 로고    scopus 로고
    • Molecular cloning of a novel gene, dtsR, which rescues the detergent sensitivity of a mutant derived from Brevibacterium lactofermentum
    • Kimura E, Abe C, Kawahara Y, Nakamatsu T (1996) Molecular cloning of a novel gene, dtsR, which rescues the detergent sensitivity of a mutant derived from Brevibacterium lactofermentum. Biosci Biotechnol Biochem 60: 1565-1570.
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 1565-1570
    • Kimura, E.1    Abe, C.2    Kawahara, Y.3    Nakamatsu, T.4
  • 30
    • 0030919128 scopus 로고    scopus 로고
    • A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiently produces l-glutamate in the presence of an excess of biotin
    • Kimura E, Abe C, Kawahara Y, Nakamatsu T, Tokuda H (1997) A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiently produces l-glutamate in the presence of an excess of biotin. Biochem Biophys Res Commun 234: 157-161.
    • (1997) Biochem Biophys Res Commun , vol.234 , pp. 157-161
    • Kimura, E.1    Abe, C.2    Kawahara, Y.3    Nakamatsu, T.4    Tokuda, H.5
  • 31
    • 0001239046 scopus 로고    scopus 로고
    • Glutamate overproduction in Corynebacterium glutamicum triggered by a decrease in the level of a complex comprising DtsR and a biotin-containing subunit
    • Kimura E, Yagoshi C, Kawahara Y, Ohsumi T, Nakamatsu T, Tokuda H (1999) Glutamate overproduction in Corynebacterium glutamicum triggered by a decrease in the level of a complex comprising DtsR and a biotin-containing subunit. Biosci Biotechnol Biochem 63: 1274-1278.
    • (1999) Biosci Biotechnol Biochem , vol.63 , pp. 1274-1278
    • Kimura, E.1    Yagoshi, C.2    Kawahara, Y.3    Ohsumi, T.4    Nakamatsu, T.5    Tokuda, H.6
  • 32
    • 0003051933 scopus 로고
    • Glutamic acid bacteria
    • Demain AL, Solomon NA (eds), Benjamin Cummings, San Francisco
    • Kinoshita S (1985) Glutamic acid bacteria. In: Demain AL, Solomon NA (eds) Biology of industrial microorganisms. Benjamin Cummings, San Francisco, pp 115-145.
    • (1985) Biology of industrial microorganisms , pp. 115-145
    • Kinoshita, S.1
  • 33
    • 85008095806 scopus 로고
    • Studies on the amino acid fermentation. Part 1. Production of L-glutamic acid by various microorganisms
    • Kinoshita S, Udaka S, Shimono M (1957) Studies on the amino acid fermentation. Part 1. Production of L-glutamic acid by various microorganisms. J Gen Appl Microbiol 50: 193-205.
    • (1957) J Gen Appl Microbiol , vol.50 , pp. 193-205
    • Kinoshita, S.1    Udaka, S.2    Shimono, M.3
  • 34
    • 58249089508 scopus 로고    scopus 로고
    • In silico genome-scale reconstruction and validation of the Corynebacterium glutamicum metabolic network
    • Kjeldsen KR, Nielsen J (2009) In silico genome-scale reconstruction and validation of the Corynebacterium glutamicum metabolic network. Biotechnol Bioeng 102: 583-597.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 583-597
    • Kjeldsen, K.R.1    Nielsen, J.2
  • 35
    • 77951297189 scopus 로고    scopus 로고
    • The FHA domain of OdhI interacts with the carboxyterminal 2-oxoglutarate dehydrogenase domain of OdhA in Corynebacterium glutamicum
    • Krawczyk S, Raasch K, Schultz C, Hoffelder M, Eggeling L, Bott M (2010) The FHA domain of OdhI interacts with the carboxyterminal 2-oxoglutarate dehydrogenase domain of OdhA in Corynebacterium glutamicum. FEBS Lett 584: 1463-1468.
    • (2010) FEBS Lett , vol.584 , pp. 1463-1468
    • Krawczyk, S.1    Raasch, K.2    Schultz, C.3    Hoffelder, M.4    Eggeling, L.5    Bott, M.6
  • 36
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • Levina N, Totemeyer S, Stokes NR, Louis P, Jones MA, Booth IR (1999) Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity. EMBO J 18: 1730-1737.
    • (1999) EMBO J , vol.18 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 37
    • 80055049166 scopus 로고    scopus 로고
    • Genome sequence of Corynebacterium glutamicum S9114, a strain for industrial production of glutamate
    • Lv Y, Wu Z, Han S, Lin Y, Zheng S (2011) Genome sequence of Corynebacterium glutamicum S9114, a strain for industrial production of glutamate. J Bacteriol 193: 6096-6097.
    • (2011) J Bacteriol , vol.193 , pp. 6096-6097
    • Lv, Y.1    Wu, Z.2    Han, S.3    Lin, Y.4    Zheng, S.5
  • 38
    • 84862907560 scopus 로고    scopus 로고
    • Genome sequence of Corynebacterium glutamicum ATCC 14067, which provides insight into amino acid biosynthesis in coryneform bacteria
    • Lv Y, Liao J, Wu Z, Han S, Lin Y, Zheng S (2012) Genome sequence of Corynebacterium glutamicum ATCC 14067, which provides insight into amino acid biosynthesis in coryneform bacteria. J Bacteriol 194: 742-743.
    • (2012) J Bacteriol , vol.194 , pp. 742-743
    • Lv, Y.1    Liao, J.2    Wu, Z.3    Han, S.4    Lin, Y.5    Zheng, S.6
  • 39
    • 34547211797 scopus 로고    scopus 로고
    • Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce L-glutamic acid production
    • Nakamura J, Hirano S, Ito H, Wachi M (2007) Mutations of the Corynebacterium glutamicum NCgl1221 gene, encoding a mechanosensitive channel homolog, induce L-glutamic acid production. Appl Environ Microbiol 73: 4491-4498.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 4491-4498
    • Nakamura, J.1    Hirano, S.2    Ito, H.3    Wachi, M.4
  • 40
    • 84910316175 scopus 로고
    • Fermentative production of L-arginine
    • Nakayama K, Yoshida H (1972) Fermentative production of L-arginine. Agric Biol Chem 36: 1675-1684.
    • (1972) Agric Biol Chem , vol.36 , pp. 1675-1684
    • Nakayama, K.1    Yoshida, H.2
  • 41
    • 85007881932 scopus 로고
    • Studies on lysine fermentation I. The control mechanism on lysine accumulation by homoserine and threonine
    • Nakayama K, Kitada S, Kinoshita S (1961) Studies on lysine fermentation I. The control mechanism on lysine accumulation by homoserine and threonine. J Gen Appl Microbiol 7: 145-154.
    • (1961) J Gen Appl Microbiol , vol.7 , pp. 145-154
    • Nakayama, K.1    Kitada, S.2    Kinoshita, S.3
  • 43
    • 0002972244 scopus 로고
    • Effect of penicillin on amino acid fermentation
    • Nara T, Samejima H, Kinoshita S (1964) Effect of penicillin on amino acid fermentation. Agric Biol Chem 28: 120-124.
    • (1964) Agric Biol Chem , vol.28 , pp. 120-124
    • Nara, T.1    Samejima, H.2    Kinoshita, S.3
  • 44
    • 33744950488 scopus 로고    scopus 로고
    • Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein
    • Niebisch A, Kabus A, Schultz C, Weil B, Bott M (2006) Corynebacterial protein kinase G controls 2-oxoglutarate dehydrogenase activity via the phosphorylation status of the OdhI protein. J Biol Chem 281: 12300-12307.
    • (2006) J Biol Chem , vol.281 , pp. 12300-12307
    • Niebisch, A.1    Kabus, A.2    Schultz, C.3    Weil, B.4    Bott, M.5
  • 47
    • 27644557271 scopus 로고    scopus 로고
    • Production of organic acids by Corynebacterium glutamicum under oxygen deprivation
    • Okino S, Inui M, Yukawa H (2005) Production of organic acids by Corynebacterium glutamicum under oxygen deprivation. Appl Microbiol Biotechnol 68: 475-480.
    • (2005) Appl Microbiol Biotechnol , vol.68 , pp. 475-480
    • Okino, S.1    Inui, M.2    Yukawa, H.3
  • 48
    • 0024512267 scopus 로고
    • Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC13032
    • O'Regan M, Thierbach G, Bachmann B, Villeval D, Lepage P, Viret JF, Lemoine Y (1989) Cloning and nucleotide sequence of the phosphoenolpyruvate carboxylase-coding gene of Corynebacterium glutamicum ATCC13032. Gene 77: 237-251.
    • (1989) Gene , vol.77 , pp. 237-251
    • O'Regan, M.1    Thierbach, G.2    Bachmann, B.3    Villeval, D.4    Lepage, P.5    Viret, J.F.6    Lemoine, Y.7
  • 49
    • 0031967783 scopus 로고    scopus 로고
    • Pyruvate carboxylase from Corynebacterium glutamicum: Characterization, expression and inactivation of the pyc gene
    • Peters-Wendisch PG, Kreutzer C, Kalinowski J, Patek M, Sahm H, Eikmanns BJ (1998) Pyruvate carboxylase from Corynebacterium glutamicum: characterization, expression and inactivation of the pyc gene. Microbiology 144(Pt 4): 915-927.
    • (1998) Microbiology , vol.144 , pp. 915-927
    • Peters-Wendisch, P.G.1    Kreutzer, C.2    Kalinowski, J.3    Patek, M.4    Sahm, H.5    Eikmanns, B.J.6
  • 52
    • 54949135760 scopus 로고    scopus 로고
    • Engineering of a glycerol utilization pathway for amino acid production by Corynebacterium glutamicum
    • Rittmann D, Lindner SN, Wendisch VF (2008) Engineering of a glycerol utilization pathway for amino acid production by Corynebacterium glutamicum. Appl Environ Microbiol 74: 6216-6222.
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6216-6222
    • Rittmann, D.1    Lindner, S.N.2    Wendisch, V.F.3
  • 53
    • 85007985083 scopus 로고
    • Microbial production of L-lysine III. Production by mutants resistant to S-(2-aminoethyl)-L-cysteine
    • Sano K, Shiio I (1970) Microbial production of L-lysine III. Production by mutants resistant to S-(2-aminoethyl)-L-cysteine. J Gen Appl Microbiol 16(1): 373-391.
    • (1970) J Gen Appl Microbiol , vol.16 , Issue.1 , pp. 373-391
    • Sano, K.1    Shiio, I.2
  • 54
    • 48449096521 scopus 로고    scopus 로고
    • Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum
    • Sato H, Orishimo K, Shirai T, Hirasawa T, Nagahisa K, Shimizu H, Wachi M (2008) Distinct roles of two anaplerotic pathways in glutamate production induced by biotin limitation in Corynebacterium glutamicum. J Biosci Bioeng 106: 51-58.
    • (2008) J Biosci Bioeng , vol.106 , pp. 51-58
    • Sato, H.1    Orishimo, K.2    Shirai, T.3    Hirasawa, T.4    Nagahisa, K.5    Shimizu, H.6    Wachi, M.7
  • 55
    • 79958698899 scopus 로고    scopus 로고
    • Production of the amino acids L-glutamate, L-lysine. L-ornithine and L-arginine from arabinose by recombinant Corynebacterium glutamicum
    • Schneider J, Niermann K, Wendisch VF (2011) Production of the amino acids L-glutamate, L-lysine. L-ornithine and L-arginine from arabinose by recombinant Corynebacterium glutamicum. J Biotechnol 154: 191-198.
    • (2011) J Biotechnol , vol.154 , pp. 191-198
    • Schneider, J.1    Niermann, K.2    Wendisch, V.F.3
  • 56
    • 34548008354 scopus 로고    scopus 로고
    • Glutamate production by Corynebacterium glutamicum: Dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG
    • Schultz C, Niebisch A, Gebel L, Bott M (2007) Glutamate production by Corynebacterium glutamicum: dependence on the oxoglutarate dehydrogenase inhibitor protein OdhI and protein kinase PknG. Appl Microbiol Biotechnol 76: 691-700.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 691-700
    • Schultz, C.1    Niebisch, A.2    Gebel, L.3    Bott, M.4
  • 57
    • 70350423494 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB. PknG and PknL of Corynebacterium glutamicum: Evidence for non-essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases
    • Schultz C, Niebisch A, Schwaiger A, Viets U, Metzger S, Bramkamp M, Bott M (2009) Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB. PknG and PknL of Corynebacterium glutamicum: evidence for non-essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases. Mol Microbiol 74: 724-741.
    • (2009) Mol Microbiol , vol.74 , pp. 724-741
    • Schultz, C.1    Niebisch, A.2    Schwaiger, A.3    Viets, U.4    Metzger, S.5    Bramkamp, M.6    Bott, M.7
  • 58
    • 0012766199 scopus 로고
    • Studies on process of glutamic acid fermentation at the enzyme level. I. On the change of α-ketoglutaric acid dehydrogenase in the course of culture
    • Shigu H, Terui G (1971) Studies on process of glutamic acid fermentation at the enzyme level. I. On the change of α-ketoglutaric acid dehydrogenase in the course of culture. J Ferm Technol 49: 400-405.
    • (1971) J Ferm Technol , vol.49 , pp. 400-405
    • Shigu, H.1    Terui, G.2
  • 59
    • 0343305594 scopus 로고
    • Microbial production of L-threonine. Part II. Production by α-amino-β-hydroxyvaleric acid resistant mutants of glutamate producing bacteria
    • Shiio I, Nakamori S (1970) Microbial production of L-threonine. Part II. Production by α-amino-β-hydroxyvaleric acid resistant mutants of glutamate producing bacteria. Agric Biol Chem 34: 448-456.
    • (1970) Agric Biol Chem , vol.34 , pp. 448-456
    • Shiio, I.1    Nakamori, S.2
  • 60
    • 0002640894 scopus 로고
    • Effect of biotin on the bacterial formation of glutamic acid. I. Glutamate formation and cellular premeability of amino acids
    • Shiio I, Otsuka SI, Takahashi M (1962) Effect of biotin on the bacterial formation of glutamic acid. I. Glutamate formation and cellular premeability of amino acids. J Biochem 51: 56-62.
    • (1962) J Biochem , vol.51 , pp. 56-62
    • Shiio, I.1    Otsuka, S.I.2    Takahashi, M.3
  • 61
    • 34548012478 scopus 로고    scopus 로고
    • Production of glutamate and glutamate-related amino acids: Molecular mechanism analysis and metabolic engineering
    • Wendisch VF (ed), Microbiology monograph, vol 5. Springer, Berlin
    • Shimizu H, Hirasawa T (2007) Production of glutamate and glutamate-related amino acids: molecular mechanism analysis and metabolic engineering. In: Wendisch VF (ed) Amino acid biosynthesis-pathways, regulation and metabolic engineering. Microbiology monograph, vol 5. Springer, Berlin, pp 1-38.
    • (2007) Amino acid biosynthesis-pathways, regulation and metabolic engineering , pp. 1-38
    • Shimizu, H.1    Hirasawa, T.2
  • 62
    • 0037350542 scopus 로고    scopus 로고
    • Effects of the changes in enzyme activities on metabolicflux redistribution around the 2-oxoglutarate branch in glutamate production by Corynebacterium glutamicum
    • Shimizu H, Tanaka H, Nakato A, Nagahisa K, Kimura E, Shioya S (2003) Effects of the changes in enzyme activities on metabolicflux redistribution around the 2-oxoglutarate branch in glutamate production by Corynebacterium glutamicum. Bioprocess Biosyst Eng 25: 291-298.
    • (2003) Bioprocess Biosyst Eng , vol.25 , pp. 291-298
    • Shimizu, H.1    Tanaka, H.2    Nakato, A.3    Nagahisa, K.4    Kimura, E.5    Shioya, S.6
  • 63
    • 69249154275 scopus 로고    scopus 로고
    • Development and experimental verification of a genome-scale metabolic model for Corynebacterium glutamicum
    • Shinfuku Y, Sorpitiporn N, Sono M, Furusawa C, Hirasawa T, Shimizu H (2009) Development and experimental verification of a genome-scale metabolic model for Corynebacterium glutamicum. Microb Cell Fact 8: 43.
    • (2009) Microb Cell Fact , vol.8
    • Shinfuku, Y.1    Sorpitiporn, N.2    Sono, M.3    Furusawa, C.4    Hirasawa, T.5    Shimizu, H.6
  • 65
    • 33845611853 scopus 로고    scopus 로고
    • Precise metabolicflux analysis of coryneform bacteria by gas chromatography-mass spectrometry and verification by nuclear magnetic resonance
    • Shirai T, Matsuzaki K, Kuzumoto M, Nagahisa K, Furusawa C, Shioya S, Shimizu H (2006) Precise metabolicflux analysis of coryneform bacteria by gas chromatography-mass spectrometry and verification by nuclear magnetic resonance. J Biosci Bioeng 102: 413-424.
    • (2006) J Biosci Bioeng , vol.102 , pp. 413-424
    • Shirai, T.1    Matsuzaki, K.2    Kuzumoto, M.3    Nagahisa, K.4    Furusawa, C.5    Shioya, S.6    Shimizu, H.7
  • 66
    • 34447620670 scopus 로고    scopus 로고
    • Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolicflux analysis
    • Shirai T, Fujimura K, Furusawa C, Nagahisa K, Shioya S, Shimizu H (2007) Study on roles of anaplerotic pathways in glutamate overproduction of Corynebacterium glutamicum by metabolicflux analysis. Microb Cell Fact 6: 19.
    • (2007) Microb Cell Fact , vol.6
    • Shirai, T.1    Fujimura, K.2    Furusawa, C.3    Nagahisa, K.4    Shioya, S.5    Shimizu, H.6
  • 68
    • 85007965705 scopus 로고
    • Biochemical effects of fatty acid and its derivatives on L-glutamic acid fermentation. Part III. Biotin-Tween 60 relationship in the accumulation of L-glutamic acid and the growth of Brevibacterium lactofermentum
    • Takinami K, Yoshii H, Tsuri H, Okada H (1965) Biochemical effects of fatty acid and its derivatives on L-glutamic acid fermentation. Part III. Biotin-Tween 60 relationship in the accumulation of L-glutamic acid and the growth of Brevibacterium lactofermentum. Agric Biol Chem 29: 351-359.
    • (1965) Agric Biol Chem , vol.29 , pp. 351-359
    • Takinami, K.1    Yoshii, H.2    Tsuri, H.3    Okada, H.4
  • 69
    • 0016584733 scopus 로고
    • Production of L-valine by 2-thiazolealanine resistant mutants derived from glutamic acid producing bacteria
    • Tsuchida T, Yoshinaga F, Kubota K, Momose H (1975) Production of L-valine by 2-thiazolealanine resistant mutants derived from glutamic acid producing bacteria. Agric Biol Chem 39: 1319-1322.
    • (1975) Agric Biol Chem , vol.39 , pp. 1319-1322
    • Tsuchida, T.1    Yoshinaga, F.2    Kubota, K.3    Momose, H.4
  • 70
  • 71
    • 72849181002 scopus 로고
    • Screening method for microorganisms accumulating metabolites and its use in the isolation of Micrococcus glutamicus
    • Udaka S (1960) Screening method for microorganisms accumulating metabolites and its use in the isolation of Micrococcus glutamicus. J Bacteriol 79: 754-755.
    • (1960) J Bacteriol , vol.79 , pp. 754-755
    • Udaka, S.1
  • 73
    • 0027572102 scopus 로고
    • Metabolicflux distributions in Corynebacterium glutamicum during growth and lysine overproduction
    • Vallino JJ, Stephanopoulos G (1993) Metabolicflux distributions in Corynebacterium glutamicum during growth and lysine overproduction. Biotechnol Bioeng 41: 633-646.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 633-646
    • Vallino, J.J.1    Stephanopoulos, G.2
  • 74
    • 33746913914 scopus 로고    scopus 로고
    • Metabolic engineering of Escherichia coli and Corynebacterium glutamicum for biotechnological production of organic acids and amino acids
    • Wendisch VF, Bott M, Eikmanns BJ (2006) Metabolic engineering of Escherichia coli and Corynebacterium glutamicum for biotechnological production of organic acids and amino acids. Curr Opin Microbiol 9: 268-274.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 268-274
    • Wendisch, V.F.1    Bott, M.2    Eikmanns, B.J.3
  • 75
    • 77950475014 scopus 로고    scopus 로고
    • Display of α-amylase on the surface of Corynebacterium glutamicum cells by using NCgl1221 as the anchoring protein, and production of glutamate from starch
    • Yao W, Chu C, Deng X, Zhang Y, Liu M, Zheng P, Sun Z (2009a) Display of α-amylase on the surface of Corynebacterium glutamicum cells by using NCgl1221 as the anchoring protein, and production of glutamate from starch. Arch Microbiol 191: 751-759.
    • (2009) Arch Microbiol , vol.191 , pp. 751-759
    • Yao, W.1    Chu, C.2    Deng, X.3    Zhang, Y.4    Liu, M.5    Zheng, P.6    Sun, Z.7
  • 76
    • 67449113538 scopus 로고    scopus 로고
    • Double deletion of dtsR1 and pyc induce efficient L-glutamate overproduction in Corynebacterium glutamicum
    • Yao W, Deng X, Zhong H, Liu M, Zheng P, Sun Z, Zhang Y (2009b) Double deletion of dtsR1 and pyc induce efficient L-glutamate overproduction in Corynebacterium glutamicum. J Ind Microbiol Biotechnol 36: 911-921.
    • (2009) J Ind Microbiol Biotechnol , vol.36 , pp. 911-921
    • Yao, W.1    Deng, X.2    Zhong, H.3    Liu, M.4    Zheng, P.5    Sun, Z.6    Zhang, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.