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Volumn 74, Issue 8, 2008, Pages 2307-2313

Differential selectivity of the Escherichia coli cell membrane shifts the equilibrium for the enzyme-catalyzed isomerization of galactose to tagatose

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENES; ISOMERIZATION;

EID: 42349089400     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02691-07     Document Type: Article
Times cited : (18)

References (30)
  • 2
    • 2442434598 scopus 로고    scopus 로고
    • A new thermophile strain of Geobacillus thermodenitrificans having L-arabinose isomerase activity for tagatose production
    • Baek, D. H., Y. Lee, H. S. Sin, and D. K. Oh. 2004. A new thermophile strain of Geobacillus thermodenitrificans having L-arabinose isomerase activity for tagatose production. J. Microbiol. Biotechnol. 14:312-316.
    • (2004) J. Microbiol. Biotechnol , vol.14 , pp. 312-316
    • Baek, D.H.1    Lee, Y.2    Sin, H.S.3    Oh, D.K.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0033010510 scopus 로고    scopus 로고
    • Crystal structure of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: Possible structural determinants of thermostability
    • Chang, C., B. C. Park, D. S. Lee, and S. W. Suh. 1999. Crystal structure of thermostable xylose isomerases from Thermus caldophilus and Thermus thermophilus: possible structural determinants of thermostability. J. Mol. Biol. 288:623-634.
    • (1999) J. Mol. Biol , vol.288 , pp. 623-634
    • Chang, C.1    Park, B.C.2    Lee, D.S.3    Suh, S.W.4
  • 5
    • 0019769532 scopus 로고
    • Energization of the transport systems for arabinose and comparison with galactose transport in Escherichia coli
    • Daruwalla, K. R., A. T. Paxton, and P. J. Henderson. 1981. Energization of the transport systems for arabinose and comparison with galactose transport in Escherichia coli. Biochem. J. 200:611-627.
    • (1981) Biochem. J , vol.200 , pp. 611-627
    • Daruwalla, K.R.1    Paxton, A.T.2    Henderson, P.J.3
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 8
    • 0022472594 scopus 로고
    • Intracellular Trp repressor levels in Escherichia coli
    • Gunsalus, R. P., A. G. Miguel, and G. L. Gunsalus. 1986. Intracellular Trp repressor levels in Escherichia coli. J. Bacteriol. 167:272-278.
    • (1986) J. Bacteriol , vol.167 , pp. 272-278
    • Gunsalus, R.P.1    Miguel, A.G.2    Gunsalus, G.L.3
  • 9
    • 0020608207 scopus 로고
    • Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning
    • Harayama, S., J. Bollinger, T. Iino, and G. L. Hazelbauer. 1983. Characterization of the mgl operon of Escherichia coli by transposon mutagenesis and molecular cloning. J. Bacteriol. 153:408-415.
    • (1983) J. Bacteriol , vol.153 , pp. 408-415
    • Harayama, S.1    Bollinger, J.2    Iino, T.3    Hazelbauer, G.L.4
  • 10
    • 3142713057 scopus 로고    scopus 로고
    • Enzymatic conversion of D-galactose to D-tagatose: Heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii
    • Jorgensen, F., O. C. Hansen, and P. Stougaard. 2004. Enzymatic conversion of D-galactose to D-tagatose: heterologous expression and characterisation of a thermostable L-arabinose isomerase from Thermoanaerobacter mathranii. Appl. Microbiol. Biotechnol. 64:816-822.
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , pp. 816-822
    • Jorgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 11
    • 23244444982 scopus 로고    scopus 로고
    • Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus L-arabinose isomerase mutant in a packed-bed bioreactor
    • Jung, E. S., H. J. Kim, and D. K. Oh. 2005. Tagatose production by immobilized recombinant Escherichia coli cells containing Geobacillus stearothermophilus L-arabinose isomerase mutant in a packed-bed bioreactor. Biotechnol. Prog. 21:1335-1340.
    • (2005) Biotechnol. Prog , vol.21 , pp. 1335-1340
    • Jung, E.S.1    Kim, H.J.2    Oh, D.K.3
  • 12
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: Bioconversion of D-galactose to D-tagatose using the enzyme
    • Kim, B. C., Y. H. Lee, H. S. Lee, D. W. Lee, E. A. Choe, and Y. R. Pyun. 2002. Cloning, expression and characterization of L-arabinose isomerase from Thermotoga neapolitana: bioconversion of D-galactose to D-tagatose using the enzyme. FEMS Microbiol. Lett. 212:121-126.
    • (2002) FEMS Microbiol. Lett , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 13
    • 33745454160 scopus 로고    scopus 로고
    • Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose
    • Kim, H. J., J. H. Kim, H. J. Oh, and D. K. Oh. 2006. Characterization of a mutated Geobacillus stearothermophilus L-arabinose isomerase that increases the production rate of D-tagatose. J. Appl. Microbiol. 101:213-221.
    • (2006) J. Appl. Microbiol , vol.101 , pp. 213-221
    • Kim, H.J.1    Kim, J.H.2    Oh, H.J.3    Oh, D.K.4
  • 14
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose
    • Kim, H. J., and D. K. Oh. 2005. Purification and characterization of an L-arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing D-tagatose. J. Biotechnol. 120:162-173.
    • (2005) J. Biotechnol , vol.120 , pp. 162-173
    • Kim, H.J.1    Oh, D.K.2
  • 15
    • 0037357583 scopus 로고    scopus 로고
    • A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • Kim, H. J., S. A. Ryu, P. Kim, and D. K. Oh. 2003. A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol. Prog. 19:400-404.
    • (2003) Biotechnol. Prog , vol.19 , pp. 400-404
    • Kim, H.J.1    Ryu, S.A.2    Kim, P.3    Oh, D.K.4
  • 16
    • 0037742418 scopus 로고    scopus 로고
    • Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. IM6501
    • Kim, J. W., Y. W. Kim, H. J. Roh, H. Y. Kim, J. H. Cha, K. H. Park, and C. S. Park. 2003. Production of tagatose by a recombinant thermostable L-arabinose isomerase from Thermus sp. IM6501. Biotechnol. Lett. 25:963-967.
    • (2003) Biotechnol. Lett , vol.25 , pp. 963-967
    • Kim, J.W.1    Kim, Y.W.2    Roh, H.J.3    Kim, H.Y.4    Cha, J.H.5    Park, K.H.6    Park, C.S.7
  • 17
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • Lee, D. W., E. A. Choe, S. B. Kim, S. H. Eom, Y. H. Hong, S. J. Lee, H. S. Lee, D. Y. Lee, and Y. R. Pyun. 2005. Distinct metal dependence for catalytic and structural functions in the L-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus. Arch. Biochem. Biophys. 434:333-343.
    • (2005) Arch. Biochem. Biophys , vol.434 , pp. 333-343
    • Lee, D.W.1    Choe, E.A.2    Kim, S.B.3    Eom, S.H.4    Hong, Y.H.5    Lee, S.J.6    Lee, H.S.7    Lee, D.Y.8    Pyun, Y.R.9
  • 18
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
    • Lee, D. W., H. J. Jang, E. A. Choe, B. C. Kim, S. J. Lee, S. B. Kim, Y. H. Hong, and Y. R. Pyun. 2004. Characterization of a thermostable L-arabinose (D-galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima. Appl. Environ. Microbiol. 70:1397-1404.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 1397-1404
    • Lee, D.W.1    Jang, H.J.2    Choe, E.A.3    Kim, B.C.4    Lee, S.J.5    Kim, S.B.6    Hong, Y.H.7    Pyun, Y.R.8
  • 19
    • 29144453887 scopus 로고    scopus 로고
    • Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: Role of Lys-269 in pH optimum
    • Lee, S. J., D. W. Lee, E. A. Choe, Y. H. Hong, S. B. Kim, B. C. Kim, and Y. R. Pyun. 2005. Characterization of a thermoacidophilic L-arabinose isomerase from Alicyclobacillus acidocaldarius: role of Lys-269 in pH optimum. Appl. Environ. Microbiol. 71:7888-7896.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 7888-7896
    • Lee, S.J.1    Lee, D.W.2    Choe, E.A.3    Hong, Y.H.4    Kim, S.B.5    Kim, B.C.6    Pyun, Y.R.7
  • 20
    • 0036011228 scopus 로고    scopus 로고
    • Tagatose, the new GRAS sweetener and health product
    • Levin, G. V. 2002. Tagatose, the new GRAS sweetener and health product. J. Med. Food 5:23-36.
    • (2002) J. Med. Food , vol.5 , pp. 23-36
    • Levin, G.V.1
  • 21
    • 0040436094 scopus 로고    scopus 로고
    • Functional and biochemical characterization of Escherichia coli sugar efflux transporters
    • Liu, J. Y., P. F. Miller, J. Willard, and E. R. Olson. 1999. Functional and biochemical characterization of Escherichia coli sugar efflux transporters. J. Biol. Chem. 274:22977-22984.
    • (1999) J. Biol. Chem , vol.274 , pp. 22977-22984
    • Liu, J.Y.1    Miller, P.F.2    Willard, J.3    Olson, E.R.4
  • 22
    • 0021099392 scopus 로고
    • Identification of the GalP galactose transport protein of Escherichia coli
    • Macpherson, A. J. S., M. C. Jones-Mortimer, P. Home, and P. J. Henderson. 1983. Identification of the GalP galactose transport protein of Escherichia coli. J. Biol. Chem. 258:4390-4396.
    • (1983) J. Biol. Chem , vol.258 , pp. 4390-4396
    • Macpherson, A.J.S.1    Jones-Mortimer, M.C.2    Home, P.3    Henderson, P.J.4
  • 24
    • 0035185226 scopus 로고    scopus 로고
    • Development of an immobilization method of L-arabinose isomerase for industrial production of tagatose
    • Oh, D. K., H. J. Kim, S. A. Ryu, and P. Kim. 2001. Development of an immobilization method of L-arabinose isomerase for industrial production of tagatose. Biotechnol. Lett. 23:1859-1862.
    • (2001) Biotechnol. Lett , vol.23 , pp. 1859-1862
    • Oh, D.K.1    Kim, H.J.2    Ryu, S.A.3    Kim, P.4
  • 25
    • 32944473444 scopus 로고    scopus 로고
    • Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans
    • Oh, H. J., H. J. Kim, and D. K. Oh. 2006. Increase in D-tagatose production rate by site-directed mutagenesis of L-arabinose isomerase from Geobacillus thermodenitrificans. Biotechnol. Lett. 28:145-149.
    • (2006) Biotechnol. Lett , vol.28 , pp. 145-149
    • Oh, H.J.1    Kim, H.J.2    Oh, D.K.3
  • 26
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic ion independent and thermoactive L-arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • Rhimi, M., and S. Bejar. 2006. Cloning, purification and biochemical characterization of metallic ion independent and thermoactive L-arabinose isomerase from the Bacillus stearothermophilus US100 strain. Biochim. Biophys. Acta 1760:191-199.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 27
    • 0347874223 scopus 로고    scopus 로고
    • Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase
    • Roh, H. J., P. Kim, Y. C. Park, and J. H. Choi. 2000. Bioconversion of D-galactose into D-tagatose by expression of L-arabinose isomerase. Biotechnol. Appl. Biochem. 31:1-4.
    • (2000) Biotechnol. Appl. Biochem , vol.31 , pp. 1-4
    • Roh, H.J.1    Kim, P.2    Park, Y.C.3    Choi, J.H.4
  • 28
    • 0346783288 scopus 로고    scopus 로고
    • Continuous D-tagatose production by immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • Ryu, S. A., C. S. Kim, H. J. Kim, D. H. Baek, and D. K. Oh. 2003. Continuous D-tagatose production by immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol. Prog. 19:1643-1647.
    • (2003) Biotechnol. Prog , vol.19 , pp. 1643-1647
    • Ryu, S.A.1    Kim, C.S.2    Kim, H.J.3    Baek, D.H.4    Oh, D.K.5
  • 29
    • 0029564145 scopus 로고
    • A family of homologous substrate-binding proteins with a broad of substrate specificity and dissimilar biological functions
    • Wu, L. F., and M. A. Mandrand-Berthelot. 1995. A family of homologous substrate-binding proteins with a broad of substrate specificity and dissimilar biological functions. Biochimie 77:744-750.
    • (1995) Biochimie , vol.77 , pp. 744-750
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 30
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • Yoon, S. H., P. Kim, and D. K. Oh. 2003. Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production. World J. Microbiol. Biotechnol. 19:47-51.
    • (2003) World J. Microbiol. Biotechnol , vol.19 , pp. 47-51
    • Yoon, S.H.1    Kim, P.2    Oh, D.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.