메뉴 건너뛰기




Volumn 143-144, Issue , 2003, Pages 533-542

Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in Escherichia coli

Author keywords

Kinetic mechanism; Medium chain dehydrogenase reductase; Stereospecificity; Xylose metabolism

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; XYLITOL DEHYDROGENASE;

EID: 0037325074     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00215-6     Document Type: Conference Paper
Times cited : (22)

References (26)
  • 4
    • 0033394642 scopus 로고    scopus 로고
    • Xylose utilisation: Cloning and characterisation of the xylitol dehydrogenase from Galactocandida mastotermitis
    • Habenicht A., Motejadded H., Kiess M., Wegerer A., Mattes R. Xylose utilisation: cloning and characterisation of the xylitol dehydrogenase from Galactocandida mastotermitis. Biol. Chem. 380:1999;1405-1411.
    • (1999) Biol. Chem. , vol.380 , pp. 1405-1411
    • Habenicht, A.1    Motejadded, H.2    Kiess, M.3    Wegerer, A.4    Mattes, R.5
  • 5
    • 0028151542 scopus 로고
    • A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including ζ-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins
    • Persson B., Zigler J.S., Jörnvall H. A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including ζ-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins. Eur. J. Biochem. 226:1994;15-22.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 15-22
    • Persson, B.1    Zigler, J.S.2    Jörnvall, H.3
  • 6
    • 0027320944 scopus 로고
    • Zinc coordination in mammalian sorbitol dehydrogenase
    • Karlsson C., Höög J.-O. Zinc coordination in mammalian sorbitol dehydrogenase. Eur. J. Biochem. 216:1993;103-107.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 103-107
    • Karlsson, C.1    Höög, J.-O.2
  • 8
    • 0035895426 scopus 로고    scopus 로고
    • Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 Å resolution
    • Banfield M.J., Salvucci M.E., Baker E.N., Smith C.A. Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 Å resolution. J. Mol. Biol. 306:2001;239-250.
    • (2001) J. Mol. Biol. , vol.306 , pp. 239-250
    • Banfield, M.J.1    Salvucci, M.E.2    Baker, E.N.3    Smith, C.A.4
  • 10
    • 0022332394 scopus 로고
    • Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases
    • Eklund H., Horjales E., Jörnvall H., Brändén C.-I., Jeffery J. Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry. 24:1985;8005-8012.
    • (1985) Biochemistry , vol.24 , pp. 8005-8012
    • Eklund, H.1    Horjales, E.2    Jörnvall, H.3    Brändén, C.-I.4    Jeffery, J.5
  • 11
    • 0342514615 scopus 로고    scopus 로고
    • Xylose metabolism in Candida intermedia: Efficient isolation and characterisation of two aldose reductases with different coenzyme specificities
    • Mayr P., Brüggler K., Kulbe K.D., Nidetzky B. Xylose metabolism in Candida intermedia: efficient isolation and characterisation of two aldose reductases with different coenzyme specificities. J. Chromatogr. B. 737:2000;195-202.
    • (2000) J. Chromatogr. B , vol.737 , pp. 195-202
    • Mayr, P.1    Brüggler, K.2    Kulbe, K.D.3    Nidetzky, B.4
  • 12
    • 0035969838 scopus 로고    scopus 로고
    • Structural and functional properties of aldose (xylose) reductase from the D-xylose-metabolizing yeast Candida tenuis
    • Nidetzky B., Mayr P., Neuhauser W., Puchberger M. Structural and functional properties of aldose (xylose) reductase from the D-xylose-metabolizing yeast Candida tenuis. Chem.-Biol. Interact. 130-132:2001;583-595.
    • (2001) Chem.-Biol. Interact. , vol.130-132 , pp. 583-595
    • Nidetzky, B.1    Mayr, P.2    Neuhauser, W.3    Puchberger, M.4
  • 13
    • 0037031248 scopus 로고    scopus 로고
    • +-dependent oxidation of secondary alcohols catalyzed by long-chain mannitol dehydrogenase from Pseudomonas fluorescens using pH and isotope effects
    • +-dependent oxidation of secondary alcohols catalyzed by long-chain mannitol dehydrogenase from Pseudomonas fluorescens using pH and isotope effects. Biochemistry. 41:2002;10158-10165.
    • (2002) Biochemistry , vol.41 , pp. 10158-10165
    • Klimacek, M.1    Nidetzky, B.2
  • 14
    • 0345384565 scopus 로고    scopus 로고
    • Utilization of xylitol dehydrogenase in a combined microbial/enzymatic process for production of xylitol from D-glucose
    • Mayer G., Kulbe K.D., Nidetzky B. Utilization of xylitol dehydrogenase in a combined microbial/enzymatic process for production of xylitol from D-glucose. Appl. Biochem. Biotechnol. 98-00:2002;577-589.
    • (2002) Appl. Biochem. Biotechnol. , vol.98 , pp. 577-589
    • Mayer, G.1    Kulbe, K.D.2    Nidetzky, B.3
  • 15
    • 0020345922 scopus 로고
    • Deuterium and tritium kinetic isotope effects on initial rates
    • Northrop D.B. Deuterium and tritium kinetic isotope effects on initial rates. Methods Enzymol. 87:1982;607-625.
    • (1982) Methods Enzymol. , vol.87 , pp. 607-625
    • Northrop, D.B.1
  • 17
    • 0017339091 scopus 로고
    • Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies
    • Cleland W.W. Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv. Enzymol. 45:1977;273-387.
    • (1977) Adv. Enzymol. , vol.45 , pp. 273-387
    • Cleland, W.W.1
  • 20
    • 0020789272 scopus 로고
    • Synergism between coenzyme and aldehyde binding to liver alcohol dehydrogenase
    • Andersson P., Kvassman J., Oldén B., Pettersson G. Synergism between coenzyme and aldehyde binding to liver alcohol dehydrogenase. Eur. J. Biochem. 133:1983;651-655.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 651-655
    • Andersson, P.1    Kvassman, J.2    Oldén, B.3    Pettersson, G.4
  • 21
    • 0021232307 scopus 로고
    • Synergism between coenzyme and alcohol binding to liver alcohol dehydrogenase
    • Andersson P., Kvassman J., Oldén B., Pettersson G. Synergism between coenzyme and alcohol binding to liver alcohol dehydrogenase. Eur. J. Biochem. 144:1984;317-324.
    • (1984) Eur. J. Biochem. , vol.144 , pp. 317-324
    • Andersson, P.1    Kvassman, J.2    Oldén, B.3    Pettersson, G.4
  • 22
    • 0021763168 scopus 로고
    • Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction
    • Andersson P., Kvassman J., Oldén B., Pettersson G. Catalytic significance of binary enzyme-aldehyde complexes in the liver alcohol dehydrogenase reaction. Eur. J. Biochem. 139:1984;519-527.
    • (1984) Eur. J. Biochem. , vol.139 , pp. 519-527
    • Andersson, P.1    Kvassman, J.2    Oldén, B.3    Pettersson, G.4
  • 23
    • 0015577980 scopus 로고
    • A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates
    • Dickinson F.M., Monger G.P. A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates. Biochem. J. 131:1973;261-270.
    • (1973) Biochem. J. , vol.131 , pp. 261-270
    • Dickinson, F.M.1    Monger, G.P.2
  • 25
    • 0013937518 scopus 로고
    • Substrate activation and inhibition in coenzyme-substrate reactions
    • Dalziel K., Dickinson F.M. Substrate activation and inhibition in coenzyme-substrate reactions. Biochem. J. 100:1966;491-500.
    • (1966) Biochem. J. , vol.100 , pp. 491-500
    • Dalziel, K.1    Dickinson, F.M.2
  • 26
    • 0003113183 scopus 로고
    • Kinetic and regulatory mechanisms of enzymes from isotope effects
    • P.F. Cook. Boca Raton: CRC Press
    • Cook P.F. Kinetic and regulatory mechanisms of enzymes from isotope effects. Cook P.F. Enzyme Mechanisms From Isotope Effects. 1991;203 CRC Press, Boca Raton.
    • (1991) Enzyme Mechanisms From Isotope Effects , pp. 203
    • Cook, P.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.