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Volumn 38, Issue , 2016, Pages 322-330

Production of para-aminobenzoate by genetically engineered Corynebacterium glutamicum and non-biological formation of an N-glucosyl byproduct

Author keywords

Aromatic compound; Fermentation; Glycation; Shikimate pathway

Indexed keywords

AROMATIC COMPOUNDS; CHEMICAL COMPOUNDS; FERMENTATION; GENES; GENETIC ENGINEERING; GLYCOSYLATION; MICROORGANISMS; MOLECULES; SUGARS;

EID: 84995467722     PISSN: 10967176     EISSN: 10967184     Source Type: Journal    
DOI: 10.1016/j.ymben.2016.07.010     Document Type: Article
Times cited : (50)

References (36)
  • 2
    • 0035209901 scopus 로고    scopus 로고
    • Metabolic engineering for microbial production of aromatic amino acids and derived compounds
    • Bongaerts, J., Krämer, M., Müller, U., Raeven, L., Wubbolts, M., Metabolic engineering for microbial production of aromatic amino acids and derived compounds. Metab. Eng. 3 (2001), 289–300.
    • (2001) Metab. Eng. , vol.3 , pp. 289-300
    • Bongaerts, J.1    Krämer, M.2    Müller, U.3    Raeven, L.4    Wubbolts, M.5
  • 3
    • 84865350728 scopus 로고    scopus 로고
    • Alleviating monoterpene toxicity using a two-phase extractive fermentation for the bioproduction of jet fuel mixtures in Saccharomyces cerevisiae
    • Brennan, T.C., Turner, C.D., Krömer, J.O., Nielsen, L.K., Alleviating monoterpene toxicity using a two-phase extractive fermentation for the bioproduction of jet fuel mixtures in Saccharomyces cerevisiae. Biotechnol. Bioeng. 109 (2012), 2513–2522.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 2513-2522
    • Brennan, T.C.1    Turner, C.D.2    Krömer, J.O.3    Nielsen, L.K.4
  • 4
    • 0029932798 scopus 로고    scopus 로고
    • Role of Amadori-modified nonenzymatically glycated serum proteins in the pathogenesis of diabetic nephropathy
    • Cohen, M.P., Ziyadeh, F.N., Role of Amadori-modified nonenzymatically glycated serum proteins in the pathogenesis of diabetic nephropathy. J. Am. Soc. Nephrol. 7 (1996), 183–190.
    • (1996) J. Am. Soc. Nephrol. , vol.7 , pp. 183-190
    • Cohen, M.P.1    Ziyadeh, F.N.2
  • 5
    • 66349102502 scopus 로고    scopus 로고
    • Identification of a cell-wall channel in the corynemycolic acid-free Gram-positive bacterium Corynebacterium amycolatum
    • Dörner, U., Schiffler, B., Lanéelle, M.A., Daffé, M., Benz, R., Identification of a cell-wall channel in the corynemycolic acid-free Gram-positive bacterium Corynebacterium amycolatum. Int. Microbiol. 12 (2009), 29–38.
    • (2009) Int. Microbiol. , vol.12 , pp. 29-38
    • Dörner, U.1    Schiffler, B.2    Lanéelle, M.A.3    Daffé, M.4    Benz, R.5
  • 6
    • 77950649821 scopus 로고    scopus 로고
    • Metabolic engineering for the production of shikimic acid in an evolved Escherichia coli strain lacking the phosphoenolpyruvate: carbohydrate phosphotransferase system
    • Escalante, A., Calderón, R., Valdivia, A., de Anda, R., Hernández, G., Ramírez, O.T., Gosset, G., Bolívar, F., Metabolic engineering for the production of shikimic acid in an evolved Escherichia coli strain lacking the phosphoenolpyruvate: carbohydrate phosphotransferase system. Microb. Cell Fact., 9, 2010, 21.
    • (2010) Microb. Cell Fact. , vol.9 , pp. 21
    • Escalante, A.1    Calderón, R.2    Valdivia, A.3    de Anda, R.4    Hernández, G.5    Ramírez, O.T.6    Gosset, G.7    Bolívar, F.8
  • 8
    • 0028171435 scopus 로고
    • A single Ser-180 mutation desensitizes feedback inhibition of the phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAHP) synthetase in Escherichia coli
    • Ger, Y.M., Chen, S.L., Chiang, H.J., Shiuan, D., A single Ser-180 mutation desensitizes feedback inhibition of the phenylalanine-sensitive 3-deoxy-d-arabino-heptulosonate 7-phosphate (DAHP) synthetase in Escherichia coli. J. Biochem. 116 (1994), 986–990.
    • (1994) J. Biochem. , vol.116 , pp. 986-990
    • Ger, Y.M.1    Chen, S.L.2    Chiang, H.J.3    Shiuan, D.4
  • 9
    • 0026640790 scopus 로고
    • Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme
    • Green, J.M., Merkel, W.K., Nichols, B.P., Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J. Bacteriol. 174 (1992), 5317–5323.
    • (1992) J. Bacteriol. , vol.174 , pp. 5317-5323
    • Green, J.M.1    Merkel, W.K.2    Nichols, B.P.3
  • 10
    • 0025737957 scopus 로고
    • p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC
    • Green, J.M., Nichols, B.P., p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC. J. Biol. Chem. 266 (1991), 12971–12975.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12971-12975
    • Green, J.M.1    Nichols, B.P.2
  • 11
    • 0025253582 scopus 로고
    • Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
    • Hartmans, S., van der Werf, M.J., de Bont, J.A., Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase. Appl. Environ. Microbiol. 56 (1990), 1347–1351.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1347-1351
    • Hartmans, S.1    van der Werf, M.J.2    de Bont, J.A.3
  • 12
    • 0041429540 scopus 로고    scopus 로고
    • Industrial production of amino acids by coryneform bacteria
    • Hermann, T., Industrial production of amino acids by coryneform bacteria. J. Biotechnol. 104 (2003), 155–172.
    • (2003) J. Biotechnol. , vol.104 , pp. 155-172
    • Hermann, T.1
  • 13
    • 84872265616 scopus 로고    scopus 로고
    • Recent structural and mechanistic insights into post-translational enzymatic glycosylation
    • Hurtado-Guerrero, R., Davies, G.J., Recent structural and mechanistic insights into post-translational enzymatic glycosylation. Curr. Opin. Chem. Biol. 16 (2012), 479–487.
    • (2012) Curr. Opin. Chem. Biol. , vol.16 , pp. 479-487
    • Hurtado-Guerrero, R.1    Davies, G.J.2
  • 14
    • 31144476958 scopus 로고    scopus 로고
    • Towards bacterial strains overproducing l-tryptophan and other aromatics by metabolic engineering
    • Ikeda, M., Towards bacterial strains overproducing l-tryptophan and other aromatics by metabolic engineering. Appl. Microbiol. Biotechnol. 69 (2006), 615–626.
    • (2006) Appl. Microbiol. Biotechnol. , vol.69 , pp. 615-626
    • Ikeda, M.1
  • 15
    • 0028406892 scopus 로고
    • Fermentative production of tryptophan by a stable recombinant strain of Corynebacterium glutamicum with a modified serine-biosynthetic pathway
    • Ikeda, M., Nakanishi, K., Kino, K., Katsumata, R., Fermentative production of tryptophan by a stable recombinant strain of Corynebacterium glutamicum with a modified serine-biosynthetic pathway. Biosci. Biotechnol. Biochem. 58 (1994), 674–678.
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 674-678
    • Ikeda, M.1    Nakanishi, K.2    Kino, K.3    Katsumata, R.4
  • 16
    • 25444479070 scopus 로고    scopus 로고
    • Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions
    • Inui, M., Kawaguchi, H., Murakami, S., Vertès, A.A., Yukawa, H., Metabolic engineering of Corynebacterium glutamicum for fuel ethanol production under oxygen-deprivation conditions. J. Mol. Microbiol. Biotechnol. 8 (2004), 243–254.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.8 , pp. 243-254
    • Inui, M.1    Kawaguchi, H.2    Murakami, S.3    Vertès, A.A.4    Yukawa, H.5
  • 17
    • 4644247295 scopus 로고    scopus 로고
    • Metabolic analysis of Corynebacterium glutamicum during lactate and succinate productions under oxygen deprivation conditions
    • Inui, M., Murakami, S., Okino, S., Kawaguchi, H., Vertès, A.A., Yukawa, H., Metabolic analysis of Corynebacterium glutamicum during lactate and succinate productions under oxygen deprivation conditions. J. Mol. Microbiol. Biotechnol. 7 (2004), 182–196.
    • (2004) J. Mol. Microbiol. Biotechnol. , vol.7 , pp. 182-196
    • Inui, M.1    Murakami, S.2    Okino, S.3    Kawaguchi, H.4    Vertès, A.A.5    Yukawa, H.6
  • 18
    • 0031972688 scopus 로고    scopus 로고
    • Identification and molecular characterization of an efflux pump involved in Pseudomonas putida S12 solvent tolerance
    • Kieboom, J., Dennis, J.J., de Bont, J.A., Zylstra, G.J., Identification and molecular characterization of an efflux pump involved in Pseudomonas putida S12 solvent tolerance. J. Biol. Chem. 273 (1998), 85–91.
    • (1998) J. Biol. Chem. , vol.273 , pp. 85-91
    • Kieboom, J.1    Dennis, J.J.2    de Bont, J.A.3    Zylstra, G.J.4
  • 19
    • 77955576962 scopus 로고    scopus 로고
    • Identification and elimination of the competing N-acetyldiaminopentane pathway for improved production of diaminopentane by Corynebacterium glutamicum
    • Kind, S., Jeong, W.K., Schröder, H., Zelder, O., Wittmann, C., Identification and elimination of the competing N-acetyldiaminopentane pathway for improved production of diaminopentane by Corynebacterium glutamicum. Appl. Environ. Microbiol. 76 (2010), 5175–5180.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 5175-5180
    • Kind, S.1    Jeong, W.K.2    Schröder, H.3    Zelder, O.4    Wittmann, C.5
  • 20
    • 0037321888 scopus 로고    scopus 로고
    • The biosynthesis of shikimate metabolites
    • Knaggs, A.R., The biosynthesis of shikimate metabolites. Nat. Prod. Rep. 20 (2003), 119–136.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 119-136
    • Knaggs, A.R.1
  • 23
    • 84897966208 scopus 로고    scopus 로고
    • Chorismate-dependent transcriptional regulation of quinate/shikimate utilization genes by LysR-type transcriptional regulator QsuR in Corynebacterium glutamicum: carbon flow control at metabolic branch point
    • Kubota, T., Tanaka, Y., Takemoto, N., Watanabe, A., Hiraga, K., Inui, M., Yukawa, H., Chorismate-dependent transcriptional regulation of quinate/shikimate utilization genes by LysR-type transcriptional regulator QsuR in Corynebacterium glutamicum: carbon flow control at metabolic branch point. Mol. Microbiol. 92 (2014), 356–368.
    • (2014) Mol. Microbiol. , vol.92 , pp. 356-368
    • Kubota, T.1    Tanaka, Y.2    Takemoto, N.3    Watanabe, A.4    Hiraga, K.5    Inui, M.6    Yukawa, H.7
  • 24
    • 84876305357 scopus 로고    scopus 로고
    • Acetone, butanol, and ethanol production from cane molasses using Clostridium beijerinckii mutant obtained by combined low-energy ion beam implantation and N-methyl-N-nitro-N-nitrosoguanidine induction
    • Li, H.G., Luo, W., Gu, Q.Y., Wang, Q., Hu, W.J., Yu, X.B., Acetone, butanol, and ethanol production from cane molasses using Clostridium beijerinckii mutant obtained by combined low-energy ion beam implantation and N-methyl-N-nitro-N-nitrosoguanidine induction. Bioresour. Technol. 137 (2013), 254–260.
    • (2013) Bioresour. Technol. , vol.137 , pp. 254-260
    • Li, H.G.1    Luo, W.2    Gu, Q.Y.3    Wang, Q.4    Hu, W.J.5    Yu, X.B.6
  • 27
    • 0024403436 scopus 로고
    • para-aminobenzoate synthesis from chorismate occurs in two steps
    • Nichols, B.P., Seibold, A.M., Doktor, S.Z., para-aminobenzoate synthesis from chorismate occurs in two steps. J. Biol. Chem. 264 (1989), 8597–8601.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8597-8601
    • Nichols, B.P.1    Seibold, A.M.2    Doktor, S.Z.3
  • 29
    • 84896089904 scopus 로고    scopus 로고
    • Bioproduction of 4-vinylphenol from corn cob alkaline hydrolyzate in two-phase extractive fermentation using free or immobilized recombinant E. coli expressing pad gene
    • Salgado, J.M., Rodríguez-Solana, R., Curiel, J.A., de Las Rivas, B., Muñoz, R., Domínguez, J.M., Bioproduction of 4-vinylphenol from corn cob alkaline hydrolyzate in two-phase extractive fermentation using free or immobilized recombinant E. coli expressing pad gene. Enzym. Microb. Technol. 58-59 (2014), 22–28.
    • (2014) Enzym. Microb. Technol. , vol.58-59 , pp. 22-28
    • Salgado, J.M.1    Rodríguez-Solana, R.2    Curiel, J.A.3    de Las Rivas, B.4    Muñoz, R.5    Domínguez, J.M.6
  • 30
    • 77955665708 scopus 로고    scopus 로고
    • Engineering Corynebacterium glutamicum for isobutanol production
    • Smith, K.M., Cho, K.M., Liao, J.C., Engineering Corynebacterium glutamicum for isobutanol production. Appl. Microbiol. Biotechnol. 87 (2010), 1045–1055.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1045-1055
    • Smith, K.M.1    Cho, K.M.2    Liao, J.C.3
  • 31
    • 84894576158 scopus 로고    scopus 로고
    • Post-translational modifications of intermediate filament proteins: mechanisms and functions
    • Snider, N.T., Omary, M.B., Post-translational modifications of intermediate filament proteins: mechanisms and functions. Nat. Rev. Mol. Cell Biol. 15 (2014), 163–177.
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 163-177
    • Snider, N.T.1    Omary, M.B.2
  • 33
    • 79953039327 scopus 로고    scopus 로고
    • A continuous and adsorptive bioprocess for efficient production of the natural aroma chemical 2-phenylethanol with yeast
    • Wang, H., Dong, Q., Meng, C., Shi, X.A., Guo, Y., A continuous and adsorptive bioprocess for efficient production of the natural aroma chemical 2-phenylethanol with yeast. Enzym. Microb. Technol. 48 (2011), 404–407.
    • (2011) Enzym. Microb. Technol. , vol.48 , pp. 404-407
    • Wang, H.1    Dong, Q.2    Meng, C.3    Shi, X.A.4    Guo, Y.5
  • 34
    • 0025647889 scopus 로고
    • p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase
    • Ye, Q.Z., Liu, J., Walsh, C.T., p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. USA. 87 (1990), 9391–9395.
    • (1990) Proc. Natl. Acad. Sci. USA. , vol.87 , pp. 9391-9395
    • Ye, Q.Z.1    Liu, J.2    Walsh, C.T.3


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