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Volumn 63, Issue 7, 1999, Pages 1274-1278

Glutamate overproduction in corynebacterium glutamicum triggered by a decrease in the level of a complex comprising dtsR and a biotin-containing subunit

Author keywords

Biotin; DtsR; Glutamate overproduction; Tween 40

Indexed keywords


EID: 0001239046     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1274     Document Type: Article
Times cited : (51)

References (27)
  • 1
    • 85008095806 scopus 로고
    • Studies on the ami-no acid fermentation: Part I. Production of L-glutamic acid by various microorganisms
    • Kinoshita, S., Udaka, S., and Shimono, M., Studies on the ami-no acid fermentation: Part I. Production of L-glutamic acid by various microorganisms. J. Gen. Appl. Microbiol., 3, 193-205 (1957).
    • (1957) J. Gen. Appl. Microbiol. , vol.3 , pp. 193-205
    • Kinoshita, S.1    Udaka, S.2    Shimono, M.3
  • 2
    • 72849181002 scopus 로고
    • Screening method for microorganisms accumulating metabolites and its use in the isolation of
    • Udaka, S., Screening method for microorganisms accumulating metabolites and its use in the isolation of Micrococcus glutami-cus. J. Bacteriol., 79, 754-755 (1960).
    • (1960) Micrococcus Glutami-Cus. J. Bacteriol. , vol.79 , pp. 754-755
    • Udaka, S.1
  • 3
    • 0025860159 scopus 로고
    • Transfer of Brevibacterium divaricatum DSM 20297T, “Brevibacterium flavum” DSM 20411, “Brevibacterium lac-tofermentum” DSM 20412 and DSM 1412, and Corynebacteri-um lilium DSM 20137T to Corynebacterium glutamicum and their distinction by rRNA gene restriction patterns
    • T to Corynebacterium glutamicum and their distinction by rRNA gene restriction patterns. Int. J. Syst. Bacteriol, 41, 255-260 (1991).
    • (1991) Int. J. Syst. Bacteriol , vol.41 , pp. 255-260
    • Liebel, W.1    Ehrmann, M.2    Ludwig, W.3    Schleifer, K.H.4
  • 4
    • 0003051933 scopus 로고
    • Glutamic acid bacteria
    • “, ”, eds. Demain, A. L., and Solomon, N. A., The Benjamin/Cummings Publishing Company, Inc., California
    • Kinoshita, S., Glutamic acid bacteria. In “Biology of industrial microorganisms”, eds. Demain, A. L., and Solomon, N. A., The Benjamin/Cummings Publishing Company, Inc., California, pp. 115-142 (1985).
    • (1985) Biology of Industrial Microorganisms , pp. 115-142
    • Kinoshita, S.1
  • 5
    • 0002530549 scopus 로고
    • Amino acids biosynthesis and genetic regulation
    • “, ”, eds., Herrmann, K. M., and Somerville, R. L., Addison-Wesley Publishing Company, London
    • Yoshinaga, F., and Nakamori, S., Amino acids biosynthesis and genetic regulation. In “Production of amino acids”, eds. Herrmann, K. M., and Somerville, R. L., Addison-Wesley Publishing Company, London, pp. 405-430 (1983).
    • (1983) Production of Amino Acids , pp. 405-430
    • Yoshinaga, F.1    Nakamori, S.2
  • 6
    • 0002640894 scopus 로고
    • Effect of biotin on the bacterial formation of glutamic acid: I. Glutamate formation and cellular permeability of amino acids
    • Shiio, I., Otsuka, S., and Takahashi, M., Effect of biotin on the bacterial formation of glutamic acid: I. Glutamate formation and cellular permeability of amino acids. J. Biochem., 51, 56-62 (1962).
    • (1962) J. Biochem. , vol.51 , pp. 56-62
    • Shiio, I.1    Otsuka, S.2    Takahashi, M.3
  • 7
    • 0001021102 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., and Okada, H., 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. Agr. Biol. Chem., 29, 351-359 (1965).
    • (1965) Agr. Biol. Chem. , vol.29 , pp. 351-359
    • Takinami, K.1    Yoshii, H.2    Tsuri, H.3    Okada, H.4
  • 8
    • 0014828434 scopus 로고
    • Product inhibition of the fermentative formation of glutamic acid
    • Nunheimer, T. D., Birnbaum, J., Ihnen, E. D., and Demain A. L., Product inhibition of the fermentative formation of glutamic acid. Appl. Microbiol., 20, 215-217 (1970).
    • (1970) Appl. Microbiol. , vol.20 , pp. 215-217
    • Nunheimer, T.D.1    Birnbaum, J.2    Ihnen, E.D.3    Demain, A.L.4
  • 9
    • 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., and Nakamatsu, T., 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).
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 1565-1570
    • Kimura, E.1    Abe, C.2    Kawahara, Y.3    Nakamatsu, T.4
  • 10
    • 0030919128 scopus 로고    scopus 로고
    • A dtsR gene-disrupted mutant of Brevibacterium lactofermetum 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., and Tokuda, H., A dtsR gene-disrupted mutant of Brevibacterium lactofermetum 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).
    • (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
  • 11
    • 0029785888 scopus 로고    scopus 로고
    • A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-car-boxyl-carrier proteins
    • Wolfgang, J., Peters-Wendisch, P. G., Kalinowski, J., and Piihler, A., A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-car-boxyl-carrier proteins. Arch. Microbiol., 166, 76-82 (1996).
    • (1996) Arch. Microbiol. , vol.166 , pp. 76-82
    • Wolfgang, J.1    Peters-Wendisch, P.G.2    Kalinowski, J.3    Piihler, A.4
  • 12
    • 0028278942 scopus 로고
    • Lipid synthesis in Mycobacteria: Characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. Tuberculosis
    • Norman, E., de Smet, K. A. L., Stoker, N. G., Ratledge, C., Wheeler, P. R., and Dale, J. W., Lipid synthesis in Mycobacteria: Characterization of the biotin carboxyl carrier protein genes from Mycobacterium leprae and M. tuberculosis. J. Bacteriol., 176, 2525-2531 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 2525-2531
    • Norman, E.1    De Smet, K.A.L.2    Stoker, N.G.3    Ratledge, C.4    Wheeler, P.R.5    Dale, J.W.6
  • 13
    • 85004613154 scopus 로고
    • Presence and regulation of α-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium
    • Shiio, I., and Ujigawα-Takeda, K., Presence and regulation of α-ketoglutarate dehydrogenase complex in a glutamate-producing bacterium, Brevibacterium flavum. Agric. Biol. Chem., 44, 1897-1904 (1980).
    • (1980) Brevibacterium Flavum. Agric. Biol. Chem. , vol.44 , pp. 1897-1904
    • Shiio, I.1    Ujigawα-Takeda, K.2
  • 15
    • 0012828195 scopus 로고
    • Significance of α-ketoglutaric dehydrogenase on the glutamic acid formation in Brevibacterium flavum
    • Shiio, I., Otsuka, S., and Takahashi, M., Significance of α-ketoglutaric dehydrogenase on the glutamic acid formation in Brevibacterium flavum. J. Biochem., 50, 164-165 (1961).
    • (1961) J. Biochem. , vol.50 , pp. 164-165
    • Shiio, I.1    Otsuka, S.2    Takahashi, M.3
  • 16
    • 0012766199 scopus 로고
    • Studies on the process of glutamic acid fermentation at the enzyme level: I. On the changes of α-ketoglutaric acid dehydrogenase in the course of culture
    • Shingu, H., and Terui, G., Studies on the process of glutamic acid fermentation at the enzyme level: I. On the changes of α-ketoglutaric acid dehydrogenase in the course of culture. J. Ferment. Technol., 49, 400-405 (1971).
    • (1971) J. Ferment. Technol. , vol.49 , pp. 400-405
    • Shingu, H.1    Terui, G.2
  • 17
    • 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., and Nakamori, S., Relationship between the glutamate production and the activity of 2-oxoglutarate dehydrogenase in Brevibacterium lactofermentum. Biosci. Biotechnol. Biochem., 61, 1109-1112 (1997).
    • (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
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0010220461 scopus 로고
    • Metabolism of propionic acid in animal tissues: VIII. Crystalline propionyl carboxylase
    • Kaziro, Y., Ochoa, S., Warner, R. C., and Chen, J.-Y., Metabolism of propionic acid in animal tissues: VIII. Crystalline propionyl carboxylase. J. Biol. Chem., 236, 1917-1923 (1961).
    • (1961) J. Biol. Chem. , vol.236 , pp. 1917-1923
    • Kaziro, Y.1    Ochoa, S.2    Warner, R.C.3    Chen, J.-Y.4
  • 22
    • 0020442441 scopus 로고
    • The subunit structure and formation of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis
    • Haase, F. C., Henrikson, K. P., Treble, D. H., and Allen, S. H. G., The subunit structure and formation of the propionyl coenzyme A carboxylase of Mycobacterium smegmatis. J. Biol. Chem., 257, 11994-11999 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 11994-11999
    • Haase, F.C.1    Henrikson, K.P.2    Treble, D.H.3    Allen, S.H.G.4
  • 23
    • 0014379130 scopus 로고
    • Alteration of permeability for the release of metabolites from microbial cell
    • Demain, A. L., and Birnbaum, J., Alteration of permeability for the release of metabolites from microbial cell. Curr. Top. Microbiol. Immunol., 46, 1-25 (1968).
    • (1968) Curr. Top. Microbiol. Immunol. , vol.46 , pp. 1-25
    • Demain, A.L.1    Birnbaum, J.2
  • 24
    • 0022438140 scopus 로고
    • The manipulation of micro-organisms for the production of secondary metabolites
    • Bunch, A. W., and Harris, R. E., The manipulation of micro-organisms for the production of secondary metabolites. Biotechnol. Genet. Engineer. Rev., 4, 117-144 (1986).
    • (1986) Biotechnol. Genet. Engineer. Rev. , vol.4 , pp. 117-144
    • Bunch, A.W.1    Harris, R.E.2
  • 26
    • 0342453448 scopus 로고
    • Isolation of cDNA clones coding for the a and p chains of human propionyl-CoA carboxylase: Chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes
    • Lamhonwah, A.-M., Barankiewicz, T. J., Willard, H. F., Mahuran, D. J., Quan, F., and Gravel, R. A., Isolation of cDNA clones coding for the a and p chains of human propionyl-CoA carboxylase: Chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc. Natl. Acad. Sci. USA, 83, 4864-4868 (1986).
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4864-4868
    • Lamhonwah, A.-M.1    Barankiewicz, T.J.2    Willard, H.F.3    Mahuran, D.J.4    Quan, F.5    Gravel, R.A.6
  • 27
    • 0026787447 scopus 로고
    • The genes encoding the two car-boxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase
    • Li, S.-J., and Cronan, Jr. J. E., The genes encoding the two car-boxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase J. Biol. Chem., 267, 16841-16847 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 16841-16847
    • Li, S.-J.1    Cronan, J.E.2


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