메뉴 건너뛰기




Volumn 47, Issue 3, 2009, Pages 351-357

Cloning, expression, and characterization of xylose reductase with higher activity from Candida tropicalis

Author keywords

Candida tropicalis; Catalytic efficiency; Coenzyme specificity; Xylose reductase

Indexed keywords

CANDIDA TROPICALIS; ESCHERICHIA COLI; SACCHAROMYCES;

EID: 68349100210     PISSN: 12258873     EISSN: 12258873     Source Type: Journal    
DOI: 10.1007/s12275-008-0225-9     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 0025787980 scopus 로고
    • Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-dependent xylose reductase-encoding gene (Xyl1) from the xylose-assimilating yeast Pichia stipitis
    • Amore, R., P. Kötter, C. Küster, M. Ciriacy, and C.P. Hollenberg. 1991. Cloning and expression in Saccharomyces cerevisiae of the NAD(P)H-dependent xylose reductase-encoding gene (Xyl1) from the xylose-assimilating yeast Pichia stipitis. Gene 109, 89-97.
    • (1991) Gene , vol.109 , pp. 89-97
    • Amore, R.1    Kötter, P.2    Küster, C.3    Ciriacy, M.4    Hollenberg, C.P.5
  • 2
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeasts by electroporation
    • Becker, D.M. and L. Guarente. 1991. High-efficiency transformation of yeasts by electroporation. Methods Enzymol. 194, 182-187.
    • (1991) Methods Enzymol , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. 1976. A rapid and sensitive method for the quantitation 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
    • 14844333166 scopus 로고    scopus 로고
    • Expression and purification of antimicrobial peptide adenoregulin with Camidated terminus in Escherichia coli
    • Cao, W., Y. Zhou, Y. Ma, Q. Luo, and D. Wei. 2005. Expression and purification of antimicrobial peptide adenoregulin with Camidated terminus in Escherichia coli. Protein Expr. Purif. 40, 404-410.
    • (2005) Protein Expr. Purif. , vol.40 , pp. 404-410
    • Cao, W.1    Zhou, Y.2    Ma, Y.3    Luo, Q.4    Wei, D.5
  • 5
    • 0342316530 scopus 로고    scopus 로고
    • Xylose utilisation: Cloning and characterisation of the xylose reductase from Candida tenuis
    • Hacker, B., A. Habenicht, M. Kiess, and R. Mattes. 1999. Xylose utilisation: cloning and characterisation of the xylose reductase from Candida tenuis. Biol. Chem. 380, 1395-1403.
    • (1999) Biol. Chem. , vol.380 , pp. 1395-1403
    • Hacker, B.1    Habenicht, A.2    Kiess, M.3    Mattes, R.4
  • 7
    • 0025139414 scopus 로고
    • Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae
    • Ho, N.W., F.P. Lin, S. Huang, P.C. Andrews, and G.T. Tsao. 1990. Purification, characterization, and amino terminal sequence of xylose reductase from Candida shehatae. Enzyme Microb. Technol. 12, 33-39.
    • (1990) Enzyme Microb. Technol. , vol.12 , pp. 33-39
    • Ho, N.W.1    Lin, F.P.2    Huang, S.3    Andrews, P.C.4    Tsao, G.T.5
  • 8
    • 0035969891 scopus 로고    scopus 로고
    • The aldo-keto reductase (AKR) superfamily: An update
    • Jez, J.M. and T.M. Penning. 2001. The aldo-keto reductase (AKR) superfamily: an update. Chem. Biol. Interact. 130-132(1-3), 499-525.
    • (2001) Chem. Biol. Interact. , vol.130-132 , Issue.1-3 , pp. 499-525
    • Jez, J.M.1    Penning, T.M.2
  • 9
    • 0038748286 scopus 로고    scopus 로고
    • Molecular characterization of a gene for aldose reductase (CbXYL1) from Candida boidinii and its expression in Saccharomyces cerevisiae
    • Kang, M.H., H. Ni, and T.W. Jeffries. 2003. Molecular characterization of a gene for aldose reductase (CbXYL1) from Candida boidinii and its expression in Saccharomyces cerevisiae. Appl. Biochem. Biotechnol. 106, 265-276.
    • (2003) Appl. Biochem. Biotechnol. , vol.106 , pp. 265-276
    • Kang, M.H.1    Ni, H.2    Jeffries, T.W.3
  • 10
    • 0037118693 scopus 로고    scopus 로고
    • The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis
    • Kavanagh, K.L., M. Klimacek, B. Nidetzky, and D.K. Wilson. 2002. The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis. Biochemistry 41, 8785-8795.
    • (2002) Biochemistry , vol.41 , pp. 8785-8795
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 11
    • 0028969384 scopus 로고
    • Purification and partial characterization of an aldo-keto reductase from Saccharomyces cerevisiae
    • Kuhn, A., C. van Zyl, A. van Tonder, and B.A. Prior. 1995. Purification and partial characterization of an aldo-keto reductase from Saccharomyces cerevisiae. Appl. Environ. Microbiol. 61, 1580-1585.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1580-1585
    • Kuhn, A.1    van Zyl, C.2    van Tonder, A.3    Prior, B.A.4
  • 13
    • 0142124355 scopus 로고    scopus 로고
    • Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis
    • Lee, J.K., B.S. Koo, and S.Y. Kim. 2003. Cloning and characterization of the xyl1 gene, encoding an NADH-preferring xylose reductase from Candida parapsilosis, and its functional expression in Candida tropicalis. Appl. Environ. Microbiol. 69, 6179-6188.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 6179-6188
    • Lee, J.K.1    Koo, B.S.2    Kim, S.Y.3
  • 14
    • 0035033208 scopus 로고    scopus 로고
    • Preliminary kinetic characterization of xylose reductase and xylitol dehydrogenase extracted from Candida guilliermondii FTI 20037 cultivated in sugarcane bagasse hydrolysate for xylitol production
    • Luciane, S., G. Maria, A. Felipe, and S. Silvio 2001. Preliminary kinetic characterization of xylose reductase and xylitol dehydrogenase extracted from Candida guilliermondii FTI 20037 cultivated in sugarcane bagasse hydrolysate for xylitol production. Appl. Biochem. Biotechnol. 91-93, 671-680.
    • (2001) Appl. Biochem. Biotechnol. , vol.91-93 , pp. 671-680
    • Luciane, S.1    Maria, G.2    Felipe, A.3    Silvio, S.4
  • 15
    • 0342514615 scopus 로고    scopus 로고
    • D-xylose metabolism by Candida intermedia: Isolation and characterisation of two forms of aldose reductase with different coenzyme specificities
    • Mayr, P., K. Bruggler, K.D. Kulbe, and B. Nidetzky 2000. D-xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities. J. Chromatogr. B. 737, 195-202.
    • (2000) J. Chromatogr. B. , vol.737 , pp. 195-202
    • Mayr, P.1    Bruggler, K.2    Kulbe, K.D.3    Nidetzky, B.4
  • 16
    • 0027818753 scopus 로고
    • Microbial pentose utilization
    • Mishra, P. and A. Singh. 1993. Microbial pentose utilization. Adv. Appl. Microbiol. 39, 91-185.
    • (1993) Adv. Appl. Microbiol. , vol.39 , pp. 91-185
    • Mishra, P.1    Singh, A.2
  • 17
    • 0030881429 scopus 로고    scopus 로고
    • NAD(P)H dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme
    • Neuhauser, W., D. Haltrich, K.D. Kulbe, and B. Nidetzky. 1997. NAD(P)H dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme. Biochem. J. 326, 683-692.
    • (1997) Biochem. J. , vol.326 , pp. 683-692
    • Neuhauser, W.1    Haltrich, D.2    Kulbe, K.D.3    Nidetzky, B.4
  • 18
    • 0347597078 scopus 로고    scopus 로고
    • Multiple forms of xylose reductase in Candida intermedia: Comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies
    • Nidetzky, B., K. Bruggler, R. Kratzer, and P. Mayr. 2003. Multiple forms of xylose reductase in Candida intermedia: comparison of their functional properties using quantitative structure-activity relationships, steady-state kinetic analysis, and pH studies. J. Agr. Food Chem. 51, 7930-7935.
    • (2003) J. Agr. Food Chem. , vol.51 , pp. 7930-7935
    • Nidetzky, B.1    Bruggler, K.2    Kratzer, R.3    Mayr, P.4
  • 19
    • 0031793031 scopus 로고    scopus 로고
    • Increase of xylitol yield by feeding xylose and glucose in Candida tropicalis
    • Oh, D.K. and S.Y. Kim. 1998. Increase of xylitol yield by feeding xylose and glucose in Candida tropicalis. Appl. Microbiol. Biot. 50, 419-425.
    • (1998) Appl. Microbiol. Biot. , vol.50 , pp. 419-425
    • Oh, D.K.1    Kim, S.Y.2
  • 20
    • 0029968714 scopus 로고    scopus 로고
    • Purification, kinetic characterization and involvement of tryptophan residue at the NADPH binding site of xylose reductase from Neurospora crassa
    • Rawat, U.B. and M.B. Rao. 1996. Purification, kinetic characterization and involvement of tryptophan residue at the NADPH binding site of xylose reductase from Neurospora crassa. Biochim. Biophys. Acta. 1293, 222-230.
    • (1996) Biochim. Biophys. Acta. , vol.1293 , pp. 222-230
    • Rawat, U.B.1    Rao, M.B.2
  • 21
    • 0021959310 scopus 로고
    • Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis
    • Verduyn, C., R. Vankleef, J. Frank, H. Schreuder, J.P. Vandijken, and W.A. Scheffers. 1985. Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis. Biochem. J. 226, 669-677.
    • (1985) Biochem. J. , vol.226 , pp. 669-677
    • Verduyn, C.1    Vankleef, R.2    Frank, J.3    Schreuder, H.4    Vandijken, J.P.5    Scheffers, W.A.6
  • 22
    • 15444371063 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa
    • Woodyer, R., M. Simurdiak, W.A. van Der Donk, and H. Zhao. 2005. Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa. Appl. Environ. Microbiol. 71, 1642-1647.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 1642-1647
    • Woodyer, R.1    Simurdiak, M.2    van der Donk, W.A.3    Zhao, H.4
  • 23
    • 0029670196 scopus 로고    scopus 로고
    • Production of xylitol from D-xylose by Candida tropicalis: The effect of D-glucose feeding
    • Yahashi, Y., H. Horitsu, K. Kawai, T. Suzuki, and K. Takamizawa. 1996. Production of xylitol from D-xylose by Candida tropicalis: the effect of D-glucose feeding. J. Ferment. Bioeng. 81, 148-152.
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 148-152
    • Yahashi, Y.1    Horitsu, H.2    Kawai, K.3    Suzuki, T.4    Takamizawa, K.5
  • 24
    • 0029417316 scopus 로고
    • Cloning and sequencing of two xylose reductase genes (xyrA and xyrB) from Candida tropicalis
    • Yokoyama, S., T. Suzuki, K. Kawai, H. Horitsu, and K. Takamizawa. 1995a. Cloning and sequencing of two xylose reductase genes (xyrA and xyrB) from Candida tropicalis. J. Ferment. Bioeng. 80, 603-605.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 603-605
    • Yokoyama, S.1    Suzuki, T.2    Kawai, K.3    Horitsu, H.4    Takamizawa, K.5
  • 25
    • 0028945054 scopus 로고
    • Purification, characterization and structure analysis of NADPH-dependent xylose reductases from Candida tropicalis
    • Yokoyama, S., T. Suzuki, K. Kawai, H. Horitsu, and K. Takamizawa. 1995b. Purification, characterization and structure analysis of NADPH-dependent xylose reductases from Candida tropicalis. J. Ferment. Bioeng. 79, 217-223.
    • (1995) J. Ferment. Bioeng. , vol.79 , pp. 217-223
    • Yokoyama, S.1    Suzuki, T.2    Kawai, K.3    Horitsu, H.4    Takamizawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.