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Volumn 74, Issue 1, 2007, Pages 22-34

Bacillus methanolicus: A candidate for industrial production of amino acids from methanol at 50°C

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOTECHNOLOGY; FERMENTATION; METHANOL; MICROORGANISMS; SUGARS;

EID: 33846607693     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0757-z     Document Type: Short Survey
Times cited : (74)

References (68)
  • 1
    • 0005046348 scopus 로고
    • Growth-characteristics of a thermotolerant methylotrophic Bacillus sp (NCIB-12522) in batch culture
    • Al-Awadhi NT, Egli T, Hamer G (1988) Growth-characteristics of a thermotolerant methylotrophic Bacillus sp (NCIB-12522) in batch culture. Appl Microbiol Biotechnol 29:485-493
    • (1988) Appl Microbiol Biotechnol , vol.29 , pp. 485-493
    • Al-Awadhi, N.T.1    Egli, T.2    Hamer, G.3
  • 2
    • 85011226423 scopus 로고
    • Thermotolerant and thermophilic solvent-utilizing methylotrophic aerobic bacteria
    • Al-Awadhi N, Egli T, Hamer G, Wehrli E (1989) Thermotolerant and thermophilic solvent-utilizing methylotrophic aerobic bacteria. Syst Appl Microbiol 11:207-216
    • (1989) Syst Appl Microbiol , vol.11 , pp. 207-216
    • Al-Awadhi, N.1    Egli, T.2    Hamer, G.3    Wehrli, E.4
  • 4
    • 0001865979 scopus 로고
    • Assimilation of carbon by methylotrophs
    • Goldberg I, Rokem JS eds, Butterworth-Heinemann, Boston
    • Anthony C (1991) Assimilation of carbon by methylotrophs. In: Goldberg I, Rokem JS (eds) Biology of methylotrophs. Butterworth-Heinemann, Boston
    • (1991) Biology of methylotrophs
    • Anthony, C.1
  • 5
    • 0024374320 scopus 로고
    • Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme
    • Arfman N, Watling EM, Clement W, van Oosterwijk RJ, de Vries GE, Harder W, Attwood MM, Dijkhuizen L (1989) Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme. Arch Microbiol 152:280-288
    • (1989) Arch Microbiol , vol.152 , pp. 280-288
    • Arfman, N.1    Watling, E.M.2    Clement, W.3    van Oosterwijk, R.J.4    de Vries, G.E.5    Harder, W.6    Attwood, M.M.7    Dijkhuizen, L.8
  • 8
    • 0031051015 scopus 로고    scopus 로고
    • Properties of a NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus
    • Arfman N, Hektor HJ, Bystrykh LV, Govorukhina NI, Dijkhuizen L, Frank J (1997) Properties of a NAD(H)-containing methanol dehydrogenase and its activator protein from Bacillus methanolicus. Eur J Biochem 244:426-433
    • (1997) Eur J Biochem , vol.244 , pp. 426-433
    • Arfman, N.1    Hektor, H.J.2    Bystrykh, L.V.3    Govorukhina, N.I.4    Dijkhuizen, L.5    Frank, J.6
  • 9
    • 0005736451 scopus 로고    scopus 로고
    • Biosynthesis of amino acids of the glutamate and aspartate families, alanine and polyamines
    • Sonenshein AL, Hoch JA, Losick R eds, ASM Press, Washington DC, pp
    • Belitsky BR (2002) Biosynthesis of amino acids of the glutamate and aspartate families, alanine and polyamines. In: Sonenshein AL, Hoch JA, Losick R (eds) Bacillus subtilis and its closest relatives: from genes to cells. ASM Press, Washington DC, pp 203-232
    • (2002) Bacillus subtilis and its closest relatives: From genes to cells , pp. 203-232
    • Belitsky, B.R.1
  • 13
    • 0000779182 scopus 로고
    • Environmental control of metabolic fluxes in thermotolerant methylotrophic Bacillus strains
    • Brooke AG, Watling EM, Attwood MM, Tempest DW (1989) Environmental control of metabolic fluxes in thermotolerant methylotrophic Bacillus strains. Arch Microbiol 151:268-273
    • (1989) Arch Microbiol , vol.151 , pp. 268-273
    • Brooke, A.G.1    Watling, E.M.2    Attwood, M.M.3    Tempest, D.W.4
  • 14
    • 0020650194 scopus 로고
    • Lysine excretion by S-(2-aminoethyl)L-cysteine resistant mutants of Bacillus subtilis
    • Chaudhuri A, Mishra AK, Nanda G (1983) Lysine excretion by S-(2-aminoethyl)L-cysteine resistant mutants of Bacillus subtilis. Acta Microbiol Pol 32:37-45
    • (1983) Acta Microbiol Pol , vol.32 , pp. 37-45
    • Chaudhuri, A.1    Mishra, A.K.2    Nanda, G.3
  • 15
    • 0030050715 scopus 로고    scopus 로고
    • Characterization of a restriction-modification system of the thermotolerant methylotroph Bacillus methanolicus
    • Cue D, Lam H, Hanson RS, Flickinger MC (1996) Characterization of a restriction-modification system of the thermotolerant methylotroph Bacillus methanolicus. Appl Environ Microbiol 62:1107-1111
    • (1996) Appl Environ Microbiol , vol.62 , pp. 1107-1111
    • Cue, D.1    Lam, H.2    Hanson, R.S.3    Flickinger, M.C.4
  • 16
    • 0031003516 scopus 로고    scopus 로고
    • Genetic manipulation of Bacillus methanolicus, a gram positive, thermotolerant methylotroph
    • Cue D, Lam H, Dillingham RL, Hanson RS, Flickinger MC (1997) Genetic manipulation of Bacillus methanolicus, a gram positive, thermotolerant methylotroph. Appl Environ Microbiol 63:1406-1420
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1406-1420
    • Cue, D.1    Lam, H.2    Dillingham, R.L.3    Hanson, R.S.4    Flickinger, M.C.5
  • 17
    • 0025157111 scopus 로고
    • Physiology and genetics of methylotrophic bacteria
    • De Vries GE, Kües U, Stahl U (1990) Physiology and genetics of methylotrophic bacteria. FEMS Microbiol Rev 6:57-102
    • (1990) FEMS Microbiol Rev , vol.6 , pp. 57-102
    • De Vries, G.E.1    Kües, U.2    Stahl, U.3
  • 18
    • 0026730941 scopus 로고
    • Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene
    • De Vries GE, Arfman N, Terpstra P, Dijkhuizen L (1992) Cloning, expression, and sequence analysis of the Bacillus methanolicus C1 methanol dehydrogenase gene. J Bacteriol 174:5346-5353
    • (1992) J Bacteriol , vol.174 , pp. 5346-5353
    • De Vries, G.E.1    Arfman, N.2    Terpstra, P.3    Dijkhuizen, L.4
  • 20
    • 0002941695 scopus 로고
    • The physiology and biochemistry of aerobic methanol-utilizing Gram-negative and Gram-positive bacteria
    • Murrell JC, Dalton H eds, Plenum, New York
    • Dijkhuizen L, Levering PR, De Vries GE (1992) The physiology and biochemistry of aerobic methanol-utilizing Gram-negative and Gram-positive bacteria. In: Murrell JC, Dalton H (eds) Methane and methanol utilizers. Plenum, New York
    • (1992) Methane and methanol utilizers
    • Dijkhuizen, L.1    Levering, P.R.2    De Vries, G.E.3
  • 22
    • 79955480846 scopus 로고    scopus 로고
    • Microbial production of L-amino acids
    • Faurie R, Thommel J eds, Springer, Berlin Heidelberg New York
    • Faurie R, Thommel J (eds) (2003) Microbial production of L-amino acids. Advances in biochemical engineering, biotechnology vol. 79. Springer, Berlin Heidelberg New York
    • (2003) Advances in biochemical engineering, biotechnology , vol.79
  • 23
    • 0032950276 scopus 로고    scopus 로고
    • Regulation of nitrogen metabolism in Bacillus subtilis: Vive la difference!
    • Fisher SH (1999) Regulation of nitrogen metabolism in Bacillus subtilis: vive la difference! Mol Microbiol 32:223-232
    • (1999) Mol Microbiol , vol.32 , pp. 223-232
    • Fisher, S.H.1
  • 24
    • 33845890355 scopus 로고    scopus 로고
    • Enhancement of L-lysine production in methylotroph Methylophilus methylotrophus by introducing a mutant lysE exporter
    • June 15
    • Gunji Y, Yasueda H (2006) Enhancement of L-lysine production in methylotroph Methylophilus methylotrophus by introducing a mutant lysE exporter. J Biotechnol June 15 127(1):1-13
    • (2006) J Biotechnol , vol.127 , Issue.1 , pp. 1-13
    • Gunji, Y.1    Yasueda, H.2
  • 25
    • 0030266252 scopus 로고    scopus 로고
    • Efficient L-serine production from methanol and glycine by resting cells of Methylobacterium sp. Strain MN43
    • Hagishita T, Yoshida T, Izumi Y, Mitsunaga T (1996) Efficient L-serine production from methanol and glycine by resting cells of Methylobacterium sp. Strain MN43. Biosci Biotechnol Biochem 60:1604-1610
    • (1996) Biosci Biotechnol Biochem , vol.60 , pp. 1604-1610
    • Hagishita, T.1    Yoshida, T.2    Izumi, Y.3    Mitsunaga, T.4
  • 27
    • 33846574940 scopus 로고    scopus 로고
    • Hanson RS, Flickinger MC, Olson P, Hur W, Al-Tahoo N, Bremmon C (2000) Production of glutamate by wild type Bacillus methanolicus US Patent 6,110,713
    • Hanson RS, Flickinger MC, Olson P, Hur W, Al-Tahoo N, Bremmon C (2000) Production of glutamate by wild type Bacillus methanolicus US Patent 6,110,713
  • 28
    • 0037033051 scopus 로고    scopus 로고
    • Identification of a magnesium-dependent NAD(P)(H)-binding domain of the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus
    • Hektor HJ, Kloosterman H, Dijkhuizen L (2002) Identification of a magnesium-dependent NAD(P)(H)-binding domain of the nicotinoprotein methanol dehydrogenase from Bacillus methanolicus. J Biol Chem 277:46966-46973
    • (2002) J Biol Chem , vol.277 , pp. 46966-46973
    • Hektor, H.J.1    Kloosterman, H.2    Dijkhuizen, L.3
  • 29
    • 0037271033 scopus 로고    scopus 로고
    • Amino acid production processes
    • Ikeda M (2003) Amino acid production processes. Adv Biochem Eng Biotechnol 79:1-35
    • (2003) Adv Biochem Eng Biotechnol , vol.79 , pp. 1-35
    • Ikeda, M.1
  • 30
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: Features and impacts on the biotechnological processes
    • Ikeda M, Nakagawa S (2003) The Corynebacterium glutamicum genome: Features and impacts on the biotechnological processes. Appl Microbiol Biotechnol 62:99-109
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 31
    • 0027272398 scopus 로고    scopus 로고
    • Izumi Y, Yoshida T, Miyazaki SS, Mitsunaga T, Oshiro T, Shimao M, Miyata A, Tanabe T (1993) L-serine production by a methylotroph and its related enzymes. Appl Microbiol Biotechnol 39:427-432
    • Izumi Y, Yoshida T, Miyazaki SS, Mitsunaga T, Oshiro T, Shimao M, Miyata A, Tanabe T (1993) L-serine production by a methylotroph and its related enzymes. Appl Microbiol Biotechnol 39:427-432
  • 32
    • 33646055513 scopus 로고    scopus 로고
    • Upregulated transcription of plasmid and chromosomal ribulose monophosphate pathway genes is critical for methanol assimilation and methanol tolerance in the methylotrophic bacterium Bacillus methanolicus
    • Jakobsen ØM, Benichou A, Flickinger MC, Valla S, Ellingsen TE, Brautaset T (2006) Upregulated transcription of plasmid and chromosomal ribulose monophosphate pathway genes is critical for methanol assimilation and methanol tolerance in the methylotrophic bacterium Bacillus methanolicus. J Bacteriol 188:3063-3072
    • (2006) J Bacteriol , vol.188 , pp. 3063-3072
    • Jakobsen, O.1    Benichou, A.2    Flickinger, M.C.3    Valla, S.4    Ellingsen, T.E.5    Brautaset, T.6
  • 34
    • 31444453261 scopus 로고    scopus 로고
    • The physiological role of the ribulose monophosphate pathway in bacteria and archaea
    • Kato N, Yurimoto H, Thauer RK (2006) The physiological role of the ribulose monophosphate pathway in bacteria and archaea. Biosci Biotechnol Biochem 70:10-21
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 10-21
    • Kato, N.1    Yurimoto, H.2    Thauer, R.K.3
  • 35
    • 0000705899 scopus 로고
    • N-succinyl-L-α,ε- diaminopimelate acid deacylase
    • Kindler SH, Gilvarg C (1960) N-succinyl-L-α,ε- diaminopimelate acid deacylase. J Biol Chem 235:3532-3535
    • (1960) J Biol Chem , vol.235 , pp. 3532-3535
    • Kindler, S.H.1    Gilvarg, C.2
  • 36
    • 0037144480 scopus 로고    scopus 로고
    • Molecular, biochemical, and functional characterization of a nudix hydrolase protein that stimulates the activity of nicotinoprotein alcohol dehydrogenase
    • Kloosterman H, Vrijbloed JW, Dijkhuizen L (2002) Molecular, biochemical, and functional characterization of a nudix hydrolase protein that stimulates the activity of nicotinoprotein alcohol dehydrogenase. J Biol Chem 277:34785-34792
    • (2002) J Biol Chem , vol.277 , pp. 34785-34792
    • Kloosterman, H.1    Vrijbloed, J.W.2    Dijkhuizen, L.3
  • 38
    • 33846612149 scopus 로고    scopus 로고
    • Kono K, Oki T, Kitai A, Ozaki A (1972) Process for producing L-glutamic acid by fermentation. US Patent 3663370
    • Kono K, Oki T, Kitai A, Ozaki A (1972) Process for producing L-glutamic acid by fermentation. US Patent 3663370
  • 40
    • 13344277347 scopus 로고    scopus 로고
    • Lysine production from methanol at 50°C using Bacillus methanolicus: Modeling volume control, lysine concentration and productivity using a three-phase continuous simulation
    • Lee GH, Hur W, Bremmon CE, Flickinger MC (1996) Lysine production from methanol at 50°C using Bacillus methanolicus: modeling volume control, lysine concentration and productivity using a three-phase continuous simulation. Biotechnol Bioeng 49:639-653
    • (1996) Biotechnol Bioeng , vol.49 , pp. 639-653
    • Lee, G.H.1    Hur, W.2    Bremmon, C.E.3    Flickinger, M.C.4
  • 41
    • 0023177784 scopus 로고
    • The potential of one-carbon compounds as fermentation feedstocks
    • Linton JD, Niekus HGD (1987) The potential of one-carbon compounds as fermentation feedstocks. Antonie Van Leeuwenhoek 53:55-63
    • (1987) Antonie Van Leeuwenhoek , vol.53 , pp. 55-63
    • Linton, J.D.1    Niekus, H.G.D.2
  • 43
    • 0027267489 scopus 로고
    • Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes
    • Mills DA, Flickinger MC (1993) Cloning and sequence analysis of the meso-diaminopimelate decarboxylase gene from Bacillus methanolicus MGA3 and comparison to other decarboxylase genes. Appl Environ Microbiol 59:2927-2937
    • (1993) Appl Environ Microbiol , vol.59 , pp. 2927-2937
    • Mills, D.A.1    Flickinger, M.C.2
  • 44
    • 0346497564 scopus 로고
    • Amino acid production from methanol by Methylobacillus glycogens mutants: Isolation of L-glutamic acid hyperproducing mutants from M. glycogens strains, and derivation of L-threonine and L-lysine-producing mutants from them
    • Motoyama H, Anazawa H, Katsumata R, Araki K, Teshiba S (1993) Amino acid production from methanol by Methylobacillus glycogens mutants: isolation of L-glutamic acid hyperproducing mutants from M. glycogens strains, and derivation of L-threonine and L-lysine-producing mutants from them. Biotechnol Biochem 57:82-87
    • (1993) Biotechnol Biochem , vol.57 , pp. 82-87
    • Motoyama, H.1    Anazawa, H.2    Katsumata, R.3    Araki, K.4    Teshiba, S.5
  • 45
    • 0027987927 scopus 로고
    • Effects of the amplification of the genes coding for the L-threonine biosynthetic enzymes of the L-threonine production from methanol by a gram negative obligate methylotroph, Methylobacillus glycogens
    • Motoyama H, Yano H, Ishino S, Anazawa H, Teshiba S (1994) Effects of the amplification of the genes coding for the L-threonine biosynthetic enzymes of the L-threonine production from methanol by a gram negative obligate methylotroph, Methylobacillus glycogens. Appl Microbiol Biotechnol 42:67-72
    • (1994) Appl Microbiol Biotechnol , vol.42 , pp. 67-72
    • Motoyama, H.1    Yano, H.2    Ishino, S.3    Anazawa, H.4    Teshiba, S.5
  • 46
    • 0035405620 scopus 로고    scopus 로고
    • Overproduction of L-lysine from methanol by Methylobacillus glycogens derivatives carrying a plasmid with a mutated dapA gene
    • Motoyama H, Yano H, Terasaki Y, Anazawa H (2001) Overproduction of L-lysine from methanol by Methylobacillus glycogens derivatives carrying a plasmid with a mutated dapA gene. Appl Environ Microbiol 67:3064-3070
    • (2001) Appl Environ Microbiol , vol.67 , pp. 3064-3070
    • Motoyama, H.1    Yano, H.2    Terasaki, Y.3    Anazawa, H.4
  • 47
    • 33846616565 scopus 로고    scopus 로고
    • Nakayama K, Kobata M, Tanaka Y, Nomura T, Katsumata R (1976) Process for the production of L-glutamic acid. US Patent 3939042
    • Nakayama K, Kobata M, Tanaka Y, Nomura T, Katsumata R (1976) Process for the production of L-glutamic acid. US Patent 3939042
  • 50
    • 0036161274 scopus 로고    scopus 로고
    • A novel methodology employing Corynebacterium glutamicum genome information to generate a new L-lysine-producing mutant
    • Ohnishi J, Mitsuhashi S, Hayashi M, Ando S, Yokoi H, Ochiai K, Ikeda M (2002) A novel methodology employing Corynebacterium glutamicum genome information to generate a new L-lysine-producing mutant. Appl Microbiol Biotechnol 58:217-223
    • (2002) Appl Microbiol Biotechnol , vol.58 , pp. 217-223
    • Ohnishi, J.1    Mitsuhashi, S.2    Hayashi, M.3    Ando, S.4    Yokoi, H.5    Ochiai, K.6    Ikeda, M.7
  • 55
    • 0026775491 scopus 로고
    • Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp
    • Schendel FJ, Flickinger MC (1992) Cloning and nucleotide sequence of the gene coding for aspartokinase II from a thermophilic methylotrophic Bacillus sp. Appl Environ Microbiol 58:2806-2814
    • (1992) Appl Environ Microbiol , vol.58 , pp. 2806-2814
    • Schendel, F.J.1    Flickinger, M.C.2
  • 56
    • 0025232281 scopus 로고    scopus 로고
    • Schendel FJ, Bremmon CE, Flickinger MC, Guettler M, Hanson RS (1990) L-Lysine production at 50°C by mutants of a newly isolated and characterized methylotrophic Bacillus sp. Appl Environ Microbiol 56:963-970
    • Schendel FJ, Bremmon CE, Flickinger MC, Guettler M, Hanson RS (1990) L-Lysine production at 50°C by mutants of a newly isolated and characterized methylotrophic Bacillus sp. Appl Environ Microbiol 56:963-970
  • 57
    • 33846605272 scopus 로고    scopus 로고
    • Schendel FJ, Dillingham R, Hanson RS, Sano K, Matsui K (2000) Production of glutamate using wild-type Bacillus methanolicus. US patent 6083728
    • Schendel FJ, Dillingham R, Hanson RS, Sano K, Matsui K (2000) Production of glutamate using wild-type Bacillus methanolicus. US patent 6083728
  • 59
    • 0020046081 scopus 로고
    • Multiple enzymic lesions in obligate methanotrophic bacteria
    • Shishkina VN, Trotsenko YA (1982) Multiple enzymic lesions in obligate methanotrophic bacteria. FEMS Microbiol Lett 13:237-242
    • (1982) FEMS Microbiol Lett , vol.13 , pp. 237-242
    • Shishkina, V.N.1    Trotsenko, Y.A.2
  • 60
    • 0007588622 scopus 로고
    • Thermophilic mixed cultures of bacteria using methanol for growth
    • Snedecor B, Cooney CL (1974) Thermophilic mixed cultures of bacteria using methanol for growth. Appl Microbiol 27:1112-1117
    • (1974) Appl Microbiol , vol.27 , pp. 1112-1117
    • Snedecor, B.1    Cooney, C.L.2
  • 61
    • 0027318885 scopus 로고
    • Flux partitioning in the split pathway of lysine in Corynebacterium glutamicum
    • Sonntag K, Eggeling L, De Graaf AA, Sahm H (1993) Flux partitioning in the split pathway of lysine in Corynebacterium glutamicum. Eur J Biochem 213:1325-1331
    • (1993) Eur J Biochem , vol.213 , pp. 1325-1331
    • Sonntag, K.1    Eggeling, L.2    De Graaf, A.A.3    Sahm, H.4
  • 62
    • 0014198941 scopus 로고
    • Biosynthesis of 2,6-diaminopimelate acid in Bacillus megaterium
    • Sundharadas G, Gilvarg C (1967) Biosynthesis of 2,6-diaminopimelate acid in Bacillus megaterium. J Biol Chem 242:2988-3983
    • (1967) J Biol Chem , vol.242 , pp. 2988-3983
    • Sundharadas, G.1    Gilvarg, C.2
  • 63
    • 0017871994 scopus 로고
    • Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum
    • Tosaka O, Takinami K (1978) Pathway and regulation of lysine biosynthesis in Brevibacterium lactofermentum. Agric Biol Chem 42:95-100
    • (1978) Agric Biol Chem , vol.42 , pp. 95-100
    • Tosaka, O.1    Takinami, K.2
  • 64
    • 33745205636 scopus 로고    scopus 로고
    • Tsujimoto N, Gunji Y, Ogawa-Miyata Y, Shimaoka M, Yasueda H (2006) L-lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer. J Biotechnol 124:327-337
    • Tsujimoto N, Gunji Y, Ogawa-Miyata Y, Shimaoka M, Yasueda H (2006) L-lysine biosynthetic pathway of Methylophilus methylotrophus and construction of an L-lysine producer. J Biotechnol 124:327-337
  • 65
    • 0031750104 scopus 로고    scopus 로고
    • Different modes of diaminopimelate synthesis and their role in cell wall integrity: A study with Corynebacterium glutamicum
    • Wehrmann A, Phillipp P, Sahm H, Eggeling L (1998) Different modes of diaminopimelate synthesis and their role in cell wall integrity: a study with Corynebacterium glutamicum. J Bacteriol 180:3159-3165
    • (1998) J Bacteriol , vol.180 , pp. 3159-3165
    • Wehrmann, A.1    Phillipp, P.2    Sahm, H.3    Eggeling, L.4
  • 66
    • 0014705659 scopus 로고
    • Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelate acid biosynthesis
    • Weinberger S, Gilvarg C (1970) Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelate acid biosynthesis. J Bacteriol 101:323-324
    • (1970) J Bacteriol , vol.101 , pp. 323-324
    • Weinberger, S.1    Gilvarg, C.2
  • 67
    • 0020683174 scopus 로고
    • The essential role of diaminopimelate dehydrogenase in the biosynthesis of lysine by Bacillus sphaericus
    • White PJ (1983) The essential role of diaminopimelate dehydrogenase in the biosynthesis of lysine by Bacillus sphaericus. J Gen Microbiol 129:739-749
    • (1983) J Gen Microbiol , vol.129 , pp. 739-749
    • White, P.J.1
  • 68
    • 33846639382 scopus 로고    scopus 로고
    • Zatman LJ (1981) A search for patterns in methylotrophic pathways. In: Dalton H (ed) Microbial growth on C1 compounds: proceedings of the Third International Symposium held in Sheffield, UK, 12-16 August 1980. Heyden London, pp 42-54
    • Zatman LJ (1981) A search for patterns in methylotrophic pathways. In: Dalton H (ed) Microbial growth on C1 compounds: proceedings of the Third International Symposium held in Sheffield, UK, 12-16 August 1980. Heyden London, pp 42-54


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