메뉴 건너뛰기




Volumn 104, Issue 1-3, 2003, Pages 199-211

Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum

Author keywords

Corynebacterium glutamicum; Diaminopimelate biosynthesis; Lysine biosynthesis; Lysine production

Indexed keywords

AMINO ACIDS; BACTERIA; BIOSYNTHESIS; GENES; PROTEINS;

EID: 0042431971     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(03)00156-1     Document Type: Article
Times cited : (47)

References (46)
  • 1
    • 0033369033 scopus 로고    scopus 로고
    • Exploiting the past and future in protein secondary structure prediction
    • Baldi P., Brunak S., Fiasconi P., Soda G. Exploiting the past and future in protein secondary structure prediction. Bioinformatics. 15:1999;937-946.
    • (1999) Bioinformatics , vol.15 , pp. 937-946
    • Baldi, P.1    Brunak, S.2    Fiasconi, P.3    Soda, G.4
  • 2
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun A., Weinstein D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70:1976;241-250.
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 3
    • 0032564314 scopus 로고    scopus 로고
    • Structural symmetry: The three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase
    • Cirilli M., Zheng R., Scapin G., Blanchard S. Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 37:1998;16452-16458.
    • (1998) Biochemistry , vol.37 , pp. 16452-16458
    • Cirilli, M.1    Zheng, R.2    Scapin, G.3    Blanchard, S.4
  • 4
    • 0025052104 scopus 로고
    • Cloning of the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum
    • Cremer J., Eggeling L., Sahm H. Cloning of the dapA dapB cluster of the lysine-secreting bacterium Corynebacterium glutamicum. Mol. Gen. Genet. 220:1990;478-480.
    • (1990) Mol. Gen. Genet. , vol.220 , pp. 478-480
    • Cremer, J.1    Eggeling, L.2    Sahm, H.3
  • 5
    • 0035232521 scopus 로고    scopus 로고
    • Metabolic engineering for L-lysine production by Corynebacterium glutamicum
    • de Graaf A.A., Eggeling L., Sahm H. Metabolic engineering for L-lysine production by Corynebacterium glutamicum. Adv. Biochem. Eng. Biotechnol. 73:2001;9-29.
    • (2001) Adv. Biochem. Eng. Biotechnol. , vol.73 , pp. 9-29
    • De Graaf, A.A.1    Eggeling, L.2    Sahm, H.3
  • 6
    • 0034044066 scopus 로고    scopus 로고
    • Characterization of a Bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-Succinyl-L,L-DAP aminotransferase
    • Fuchs T.M., Schneider B., Krumbach K., Eggeling L., Gross R. Characterization of a Bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-Succinyl-L,L-DAP aminotransferase. J. Bacteriol. 182:2000;3626-3631.
    • (2000) J. Bacteriol. , vol.182 , pp. 3626-3631
    • Fuchs, T.M.1    Schneider, B.2    Krumbach, K.3    Eggeling, L.4    Gross, R.5
  • 7
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant S., Jessee G.J., Bloom F.R., Hanahan D. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc. Natl. Acad. Sci. USA. 87:1990;4645-4649.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4645-4649
    • Grant, S.1    Jessee, G.J.2    Bloom, F.R.3    Hanahan, D.4
  • 8
    • 0031948145 scopus 로고    scopus 로고
    • LION and Degussa apply genomics to fermentation
    • Hodgson J. LION and Degussa apply genomics to fermentation. Nat. Biotechnol. 16:1998;715.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 715
    • Hodgson, J.1
  • 9
    • 0029285787 scopus 로고
    • PCR-mediated recombination and mutagenesis-SOEing together tailor-made genes
    • Horton R.M. PCR-mediated recombination and mutagenesis-SOEing together tailor-made genes. Mol. Biotechnol. 3:1995;93-99.
    • (1995) Mol. Biotechnol. , vol.3 , pp. 93-99
    • Horton, R.M.1
  • 10
    • 0023650855 scopus 로고
    • Nucleotide sequence of the meso-diaminopimelate D-dehydrogenase gene from Corynebacterium glutamicum
    • Ishino S., Mizukami Z., Yamaguchi K., Katsumata R., Araki K. Nucleotide sequence of the meso-diaminopimelate D-dehydrogenase gene from Corynebacterium glutamicum. Nucleic Acids Res. 15:1987;3917.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 3917
    • Ishino, S.1    Mizukami, Z.2    Yamaguchi, K.3    Katsumata, R.4    Araki, K.5
  • 11
    • 0020972316 scopus 로고
    • O-Phthaldialdehyde precolumn derivatization and reversed-phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids
    • Jones B.N., Gilligan J.P. o-Phthaldialdehyde precolumn derivatization and reversed-phase high-performance liquid chromatography of polypeptide hydrolysates and physiological fluids. J. Chromatogr. 266:1983;471-482.
    • (1983) J. Chromatogr. , vol.266 , pp. 471-482
    • Jones, B.N.1    Gilligan, J.P.2
  • 12
    • 0025697281 scopus 로고
    • Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum
    • Kalinowski J., Bachmann B., Thierbach G., Pühler A. Aspartokinase genes lysCα and lysCβ overlap and are adjacent to the aspartate β-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum. Mol. Gen. Genet. 224:1990;317-324.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 317-324
    • Kalinowski, J.1    Bachmann, B.2    Thierbach, G.3    Pühler, A.4
  • 13
  • 14
    • 0021278824 scopus 로고
    • Protoplast transformation of glutamate-producing bacteria with plasmid DNA
    • Katsumata R., Ozaki A., Oka T., Furuya A. Protoplast transformation of glutamate-producing bacteria with plasmid DNA. J. Bacteriol. 159:1984;306-311.
    • (1984) J. Bacteriol. , vol.159 , pp. 306-311
    • Katsumata, R.1    Ozaki, A.2    Oka, T.3    Furuya, A.4
  • 15
    • 0027164654 scopus 로고
    • Isoleucine synthesis in Corynebacterium glutamicum: Molecular analysis of the ilvB-ilvN-ilvC operon
    • Keilhauer C., Eggeling L., Sahm H. Isoleucine synthesis in Corynebacterium glutamicum: molecular analysis of the ilvB-ilvN-ilvC operon. J. Bacteriol. 175:1993;5595-5603.
    • (1993) J. Bacteriol. , vol.175 , pp. 5595-5603
    • Keilhauer, C.1    Eggeling, L.2    Sahm, H.3
  • 16
    • 0000705899 scopus 로고
    • N-succinyl-L-α,ε-diaminopimelic acid deacylase
    • Kindler S.H., Gilvarg C. N-succinyl-L-α,ε-diaminopimelic acid deacylase. J. Biol. Chem. 235:1960;3532-3535.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3532-3535
    • Kindler, S.H.1    Gilvarg, C.2
  • 17
    • 0041429497 scopus 로고    scopus 로고
    • Tools for genetic engineering in the amino acid-producing bacterium Corynebacterium glutamicu
    • in press
    • Kirchner, O., Tauch, A., 2003. Tools for genetic engineering in the amino acid-producing bacterium Corynebacterium glutamicu. J. Biotechnol. 104, in press.
    • (2003) J. Biotechnol. , vol.104
    • Kirchner, O.1    Tauch, A.2
  • 18
    • 0033528712 scopus 로고    scopus 로고
    • Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase
    • Koo C.W., Blanchard J.S. Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 38:1999;4416-4422.
    • (1999) Biochemistry , vol.38 , pp. 4416-4422
    • Koo, C.W.1    Blanchard, J.S.2
  • 19
    • 0033537677 scopus 로고    scopus 로고
    • The dual capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis
    • Ledwidge R., Blanchard J.S. The dual capability of N-acetylornithine aminotransferase in arginine and lysine biosynthesis. Biochemistry. 38:1999;3019-3024.
    • (1999) Biochemistry , vol.38 , pp. 3019-3024
    • Ledwidge, R.1    Blanchard, J.S.2
  • 20
    • 84978701453 scopus 로고    scopus 로고
    • Amino acids - Technical production and use
    • H.J. Rehm, G. Reed, A. Puehler, & P. Stadler. Weinheim, Germany: VCH
    • Leuchtenberger W. Amino acids - technical production and use. Rehm H.J., Reed G., Puehler A., Stadler P. Biotechnology. 6:1996;465-502 VCH, Weinheim, Germany.
    • (1996) Biotechnology , vol.6 , pp. 465-502
    • Leuchtenberger, W.1
  • 21
    • 0024549244 scopus 로고
    • Influence of aspartate availability on lysine formation by a recombinant strain of Corynebacterium glutamicum and utilization of fumarate
    • Menkel E., Thierbach G., Eggeling L., Sahm H. Influence of aspartate availability on lysine formation by a recombinant strain of Corynebacterium glutamicum and utilization of fumarate. Appl. Environ. Microbiol. 55:1989;684-688.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 684-688
    • Menkel, E.1    Thierbach, G.2    Eggeling, L.3    Sahm, H.4
  • 22
    • 0019200630 scopus 로고
    • Properties of meso-diaminopimelate D-dehydrogenase from Bacillus sphaericus
    • Misono H., Soda K. Properties of meso-diaminopimelate D-dehydrogenase from Bacillus sphaericus. J. Biol. Chem. 255:1980;10599-10605.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10599-10605
    • Misono, H.1    Soda, K.2
  • 23
    • 0031054312 scopus 로고    scopus 로고
    • Plasmid pGA1 from Corynebacterium glutamicum codes for a gene product that positively influences plasmid copy number
    • Nesvera J., Patek M., Hochmannova J., Abrhamova Z., Becvarova V., Jelinkova M., Vohradsky J. Plasmid pGA1 from Corynebacterium glutamicum codes for a gene product that positively influences plasmid copy number. J. Bacteriol. 179:1997;1525-1532.
    • (1997) J. Bacteriol. , vol.179 , pp. 1525-1532
    • Nesvera, J.1    Patek, M.2    Hochmannova, J.3    Abrhamova, Z.4    Becvarova, V.5    Jelinkova, M.6    Vohradsky, J.7
  • 24
    • 0036161274 scopus 로고    scopus 로고
    • A novel methodology employing Corynebacterium glutamicum genome information to generate a new L-lysine producing mutant
    • Onishi J., Mitsuhashi S., Hayashi M., Ando S., Yokoi H., Ochiai K., Ikeda M. A novel methodology employing Corynebacterium glutamicum genome information to generate a new L-lysine producing mutant. Appl. Microbiol. Biotechnol. 58:2002;217-223.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 217-223
    • Onishi, J.1    Mitsuhashi, S.2    Hayashi, M.3    Ando, S.4    Yokoi, H.5    Ochiai, K.6    Ikeda, M.7
  • 25
    • 0001501761 scopus 로고    scopus 로고
    • Biosynthesis of threonine and lysine
    • F.C. Neidhardt, R. III Curtiss, J.L. Ingraham, E.C.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, Umbarger H.E. Washington, DC: ASM Press
    • Patte J.P. Biosynthesis of threonine and lysine. Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella - Cellular and Molecular Biology. 1:1996;528-541 ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella - Cellular and Molecular Biology , vol.1 , pp. 528-541
    • Patte, J.P.1
  • 27
    • 0024284727 scopus 로고
    • Nucleotide sequence of the dapF gene and flanking regions from Escherichia coli K12
    • Richaud C., Printz C. Nucleotide sequence of the dapF gene and flanking regions from Escherichia coli K12. Nucleic Acids Res. 16:1988;10367.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10367
    • Richaud, C.1    Printz, C.2
  • 28
    • 0023234641 scopus 로고
    • Molecular cloning, characterization and chromosomal localization of dapF, the Escherichia coli gene for diaminopimelate epimerase
    • Richaud C., Higgins W., Mengin-Lecreulx D., Stragier P. Molecular cloning, characterization and chromosomal localization of dapF, the Escherichia coli gene for diaminopimelate epimerase. J. Bacteriol. 169:1987;1454-1459.
    • (1987) J. Bacteriol. , vol.169 , pp. 1454-1459
    • Richaud, C.1    Higgins, W.2    Mengin-Lecreulx, D.3    Stragier, P.4
  • 29
    • 0033782932 scopus 로고    scopus 로고
    • Pathway analysis and metabolic engineering in Corynebacterium glutamicum
    • Sahm H., Eggeling L., de Graaf A.A. Pathway analysis and metabolic engineering in Corynebacterium glutamicum. Biol. Chem. 381:2000;899-910.
    • (2000) Biol. Chem. , vol.381 , pp. 899-910
    • Sahm, H.1    Eggeling, L.2    De Graaf, A.A.3
  • 32
    • 0029958658 scopus 로고    scopus 로고
    • Three-dimensional structure of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum
    • Scapin G., Sreelatha G.R., Blanchard J.S. Three-dimensional structure of meso-diaminopimelate dehydrogenase from Corynebacterium glutamicum. Biochemistry. 35:1996;13540-13551.
    • (1996) Biochemistry , vol.35 , pp. 13540-13551
    • Scapin, G.1    Sreelatha, G.R.2    Blanchard, J.S.3
  • 33
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer A., Tauch A., Jäger W., Kalinowski J., Thierbach G., Pühler A. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene. 145:1994;69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 35
    • 0027318885 scopus 로고
    • Flux partitioning in the split pathway of lysine synthesis in Corynebacterium glutamicum
    • Sonntag K., Eggeling L., de Graaf A.A., Sahm H. Flux partitioning in the split pathway of lysine synthesis in Corynebacterium glutamicum. Eur. J. Biochem. 123:1993;1325-1331.
    • (1993) Eur. J. Biochem. , vol.123 , pp. 1325-1331
    • Sonntag, K.1    Eggeling, L.2    De Graaf, A.A.3    Sahm, H.4
  • 36
    • 0028051630 scopus 로고
    • Corynebacterium glutamicum DNA is subjected to methylation-restriction in Escherichia coli
    • Tauch A., Kirchner O., Wehmeier L., Kalinowski J., Pühler A. Corynebacterium glutamicum DNA is subjected to methylation-restriction in Escherichia coli. FEMS Microbiol. Lett. 123:1994;343-348.
    • (1994) FEMS Microbiol. Lett. , vol.123 , pp. 343-348
    • Tauch, A.1    Kirchner, O.2    Wehmeier, L.3    Kalinowski, J.4    Pühler, A.5
  • 37
    • 0029133105 scopus 로고
    • The Corynebacterium xerosis composite transposon Tn5432 consists of two identical insertion sequences, designated IS1249, flanking the erythromycin resistance gene ermCX
    • Tauch A., Kassing F., Kalinowski J., Pühler A. The Corynebacterium xerosis composite transposon Tn5432 consists of two identical insertion sequences, designated IS1249, flanking the erythromycin resistance gene ermCX. Plasmid. 34:1995;119-131.
    • (1995) Plasmid , vol.34 , pp. 119-131
    • Tauch, A.1    Kassing, F.2    Kalinowski, J.3    Pühler, A.4
  • 39
    • 0036835575 scopus 로고    scopus 로고
    • Efficient electrotransformation of Corynebacterium diphtheriae with a mini-replicon derived from the Corynebacterium glutamicum plasmid pGA1
    • Tauch A., Kirchner O., Löffler B., Götker S., Pühler A., Kalinowski J. Efficient electrotransformation of Corynebacterium diphtheriae with a mini-replicon derived from the Corynebacterium glutamicum plasmid pGA1. Curr. Microbiol. 45:2002;362-367.
    • (2002) Curr. Microbiol. , vol.45 , pp. 362-367
    • Tauch, A.1    Kirchner, O.2    Löffler, B.3    Götker, S.4    Pühler, A.5    Kalinowski, J.6
  • 40
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 0029818343 scopus 로고    scopus 로고
    • A new type of transporter with a new type of cellular function: L-lysine export from Corynebacterium glutamicum
    • Vrljic M., Sahm H., Eggeling L. A new type of transporter with a new type of cellular function: L-lysine export from Corynebacterium glutamicum. Mol. Microbiol. 22:1996;815-826.
    • (1996) Mol. Microbiol. , vol.22 , pp. 815-826
    • Vrljic, M.1    Sahm, H.2    Eggeling, L.3
  • 42
    • 0028596945 scopus 로고
    • Analysis of different DNA fragments of Corynebacterium glutamicum complementing dapE of Escherichia coli
    • Wehrmann A., Eggeling L., Sahm H. Analysis of different DNA fragments of Corynebacterium glutamicum complementing dapE of Escherichia coli. Microbiology. 140:1994;3349-3356.
    • (1994) Microbiology , vol.140 , pp. 3349-3356
    • Wehrmann, A.1    Eggeling, L.2    Sahm, H.3
  • 43
    • 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 B., Sahm H., Eggeling L. Different modes of diaminopimelate synthesis and their role in cell wall integrity: a study with Corynebacterium glutamicum. J. Bacteriol. 180:1998;3159-3165.
    • (1998) J. Bacteriol. , vol.180 , pp. 3159-3165
    • Wehrmann, A.1    Phillipp, B.2    Sahm, H.3    Eggeling, L.4
  • 44
    • 0014705659 scopus 로고
    • Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelic acid biosynthesis
    • Weinberger S., Gilvarg C. Bacterial distribution of the use of succinyl and acetyl blocking groups in diaminopimelic acid biosynthesis. J. Bacteriol. 101:1970;323-324.
    • (1970) J. Bacteriol. , vol.101 , pp. 323-324
    • Weinberger, S.1    Gilvarg, C.2
  • 45
    • 0021135333 scopus 로고
    • Purification and properties of diaminopimelic acid epimerase from Escherichia coli
    • Wiseman J.S., Nichols J.S. Purification and properties of diaminopimelic acid epimerase from Escherichia coli. J. Biol. Chem. 259:1984;8907-8914.
    • (1984) J. Biol. Chem. , vol.259 , pp. 8907-8914
    • Wiseman, J.S.1    Nichols, J.S.2
  • 46
    • 0023917918 scopus 로고
    • General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum
    • Yeh P., Sicard A., Sinskey A. General organization of the genes specifically involved in the diaminopimelate-lysine biosynthetic pathway of Corynebacterium glutamicum. Mol. Gen. Genet. 212:1988;105-111.
    • (1988) Mol. Gen. Genet. , vol.212 , pp. 105-111
    • Yeh, P.1    Sicard, A.2    Sinskey, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.