메뉴 건너뛰기




Volumn 66, Issue 1, 2002, Pages 85-91

Effects of GroESL coexpression on the folding of nicotinoprotein formaldehyde dismutase from pseudomonas putida F61

Author keywords

Formaldehyde dismutase; GroESL; Inclusion body; Molecular chaperon; Nicotinoprotein

Indexed keywords

ESCHERICHIA COLI; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0036363262     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.85     Document Type: Article
Times cited : (20)

References (24)
  • 2
    • 0021126724 scopus 로고
    • Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61
    • Kato, N., Kobayashi, H., Shimao, M., and Sakazawa, C., Properties of formaldehyde dismutation catalyzing enzyme of Pseudomonas putida F61. Agric. Biol. Chem., 48, 2017-2023 (1984).
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2017-2023
    • Kato, N.1    Kobayashi, H.2    Shimao, M.3    Sakazawa, C.4
  • 3
    • 0022483312 scopus 로고
    • Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61
    • Kato, N., Yamagami, T., Shimao, M., and Sakazawa, C., Formaldehyde dismutase, a novel NAD-binding oxidoreductase from Pseudomonas putida F61. Eur. J. Biochem., 156, 59-64 (1986).
    • (1986) Eur. J. Biochem. , vol.156 , pp. 59-64
    • Kato, N.1    Yamagami, T.2    Shimao, M.3    Sakazawa, C.4
  • 4
    • 0023153644 scopus 로고
    • Regeneration of NAD(H) covalently bound to formate dehydrogenase with several second enzymes
    • Kato, N., Yamagami, T., Shimao, M., and Sakazawa, C., Regeneration of NAD(H) covalently bound to formate dehydrogenase with several second enzymes. Appl. Microbiol. Biotechnol., 25, 415-418 (1987).
    • (1987) Appl. Microbiol. Biotechnol. , vol.25 , pp. 415-418
    • Kato, N.1    Yamagami, T.2    Shimao, M.3    Sakazawa, C.4
  • 5
    • 4544276457 scopus 로고
    • Formate production from methanol by formaldehyde dismutase coupled with a methanol oxidation system
    • Kato, N., Mizuno, S., Imada, Y., Shimao, M., and Sakazawa, C., Formate production from methanol by formaldehyde dismutase coupled with a methanol oxidation system. Appl. Microbiol. Biotechnol., 27, 567-571 (1988).
    • (1988) Appl. Microbiol. Biotechnol. , vol.27 , pp. 567-571
    • Kato, N.1    Mizuno, S.2    Imada, Y.3    Shimao, M.4    Sakazawa, C.5
  • 6
    • 0027182927 scopus 로고
    • Refolding of yeast enolase in the presence of the chapronin GroE
    • Kubo, T., Mizobata, T., and Kawata, Y., Refolding of yeast enolase in the presence of the chapronin GroE. J. Biol. Chem., 268, 19346-19351 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 19346-19351
    • Kubo, T.1    Mizobata, T.2    Kawata, Y.3
  • 7
    • 0029838899 scopus 로고    scopus 로고
    • In vivo and in vitro folding of a recombinant metalloenzyme, phos-phomannose isomerase
    • Proudfoot, A. E. I., Goffin, L., Payton, M. A., Weels, T. N. C., and Bernard, A. R., In vivo and in vitro folding of a recombinant metalloenzyme, phos-phomannose isomerase. Biochem. J., 318, 437-442 (1996).
    • (1996) Biochem. J. , vol.318 , pp. 437-442
    • Proudfoot, A.E.I.1    Goffin, L.2    Payton, M.A.3    Weels, T.N.C.4    Bernard, A.R.5
  • 8
    • 0028793115 scopus 로고
    • Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin
    • Yasukawa, T., Kanei-Ishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T., and Ishii, S., Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem., 270, 25328-25331 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 25328-25331
    • Yasukawa, T.1    Kanei-Ishii, C.2    Maekawa, T.3    Fujimoto, J.4    Yamamoto, T.5    Ishii, S.6
  • 10
    • 0031051273 scopus 로고    scopus 로고
    • GroE assists refolding of recombinant human pro-urokinase
    • Xu, Z., Yang, S., and Zhu, D., GroE assists refolding of recombinant human pro-urokinase. J. Biochem., 121, 331-337 (1997).
    • (1997) J. Biochem. , vol.121 , pp. 331-337
    • Xu, Z.1    Yang, S.2    Zhu, D.3
  • 11
    • 15844395096 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins
    • Thomas, J. G. and Baneyx, F., Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J. Biol. Chem., 271, 11141-11147 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Baneyx, F.2
  • 12
    • 0024578552 scopus 로고
    • GroE heatshock protein promoters assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli
    • Goloubiniff, P., Gantenby, A. A., and Lorimer, G. H., GroE heatshock protein promoters assembly of foreign prokaryotic ribulose biphosphate carboxylase oligomers in Escherichia coli. Nature, 337, 44-47 (1989).
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubiniff, P.1    Gantenby, A.A.2    Lorimer, G.H.3
  • 13
    • 0026726710 scopus 로고
    • Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli
    • Lee, S. C. and Olins, P. O., Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli. J. Biol. Chem., 267, 2849-2852 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 2849-2852
    • Lee, S.C.1    Olins, P.O.2
  • 14
    • 0026568947 scopus 로고
    • DnaK-mediated alterations in human growth-hormone protein inclusion body
    • Blum, P., Velligan, M., Lin, N., and Matin, A., DnaK-mediated alterations in human growth-hormone protein inclusion body. Bio/Technology, 10, 301-304 (1992).
    • (1992) Bio/Technology , vol.10 , pp. 301-304
    • Blum, P.1    Velligan, M.2    Lin, N.3    Matin, A.4
  • 15
    • 85007768156 scopus 로고
    • Cloning, sequence analysis, and expression of the gene encoding formaldehyde dismutase from Pseudo-monasputida F61
    • Yanase, H., Noda, K., Aoki, K., Kita, K., and Kato, N., Cloning, sequence analysis, and expression of the gene encoding formaldehyde dismutase from Pseudo-monasputida F61. Biosci. Biotechnol. Biochem., 59, 197-202 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 197-202
    • Yanase, H.1    Noda, K.2    Aoki, K.3    Kita, K.4    Kato, N.5
  • 16
    • 0026640258 scopus 로고
    • Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli—Refolding is enhanced in the presence of ADP
    • Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N., and Kawata, Y., Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli—Refolding is enhanced in the presence of ADP. J. Biol. Chem., 267, 17773-17779 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 17773-17779
    • Mizobata, T.1    Akiyama, Y.2    Ito, K.3    Yumoto, N.4    Kawata, Y.5
  • 17
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W. A., Kashi, Y., Furtak, K., and Horwich, A. L., Residues in chaperonin GroEL required for polypeptide binding and release. Nature, 371, 614-619 (1994).
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 18
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton W. A. and Horwich, A. L., GroEL-mediated protein folding. Protein Sci., 6, 743-760 (1997).
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 19
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B. and Horwich, A. L., The Hsp70 and Hsp60 chaperone machines. Cell, 92, 351-366 (1998).
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 20
    • 0014690454 scopus 로고
    • The enzymes of the galactose operon in Escherichia coli. II. The subunits of uridine diphosphogalactose 4-epimerase
    • Wilson, D. B. and Hogness, D. S., The enzymes of the galactose operon in Escherichia coli. II. The subunits of uridine diphosphogalactose 4-epimerase. J. Biol. Chem., 244, 2132-2236 (1966).
    • (1966) J. Biol. Chem. , vol.244 , pp. 2132-2236
    • Wilson, D.B.1    Hogness, D.S.2
  • 21
    • 0020347529 scopus 로고
    • Lactate-oxaloacetate transhydrogenase from Veillonella alcalescens
    • Allen, S. H., Lactate-oxaloacetate transhydrogenase from Veillonella alcalescens. Methods Enzymol., 89, 367-76 (1982).
    • (1982) Methods Enzymol. , vol.89 , pp. 367-376
    • Allen, S.H.1
  • 22
    • 0022497812 scopus 로고
    • Glucose-fructose oxidoreductase, a new enzyme isolated from Zymo-monas mobilis that is responsible for sorbitol production
    • Zachariou, M. and Scopes, R. K., Glucose-fructose oxidoreductase, a new enzyme isolated from Zymo-monas mobilis that is responsible for sorbitol production. J. Bacteriol., 167, 863-869 (1986).
    • (1986) J. Bacteriol. , vol.167 , pp. 863-869
    • Zachariou, M.1    Scopes, R.K.2
  • 23
    • 0030758688 scopus 로고    scopus 로고
    • Tetrazolium dye-linked alcohol dehydrogenase of the methylotrophic actinomycete Amycolaptopsis methanolica is a three-component complex
    • Bystrykh, L. V., Govorukhina, N. I., Diikhuzen, L., and Duine, J. A., Tetrazolium dye-linked alcohol dehydrogenase of the methylotrophic actinomycete Amycolaptopsis methanolica is a three-component complex. Eur. J. Biochem., 247, 280-287 (1997).
    • (1997) Eur. J. Biochem. , vol.247 , pp. 280-287
    • Bystrykh, L.V.1    Govorukhina, N.I.2    Diikhuzen, L.3    Duine, J.A.4
  • 24
    • 0030794766 scopus 로고    scopus 로고
    • Purification and characterization of an alcohol: N, N-dimethyl-4-nitrosoaniline oxidoreductase from the methanogen Methanosarcina barkeri DSM 804 strain Fusaro
    • Daussmann, T., Aivasidis, A., and Wanderey, C., Purification and characterization of an alcohol: N, N-dimethyl-4-nitrosoaniline oxidoreductase from the methanogen Methanosarcina barkeri DSM 804 strain Fusaro. Eur. J. Biochem., 248, 889-896 (1997).
    • (1997) Eur. J. Biochem. , vol.248 , pp. 889-896
    • Daussmann, T.1    Aivasidis, A.2    Wanderey, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.