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Volumn 6, Issue , 2007, Pages

Altering coenzyme specificity of Pichia stipitis xylose reductase by the semi-rational approach CASTing

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE; FUNGAL ENZYME; NITRATE REDUCTASE (NADPH); OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; XYLOSE; XYLOSE REDUCTASE;

EID: 38649127524     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-6-36     Document Type: Article
Times cited : (74)

References (32)
  • 1
    • 0027395082 scopus 로고
    • Xylose fermentation by Saccharomyces cerevisiae
    • Kötter P Ciriacy M Xylose fermentation by Saccharomyces cerevisiae Appl Microbiol Biotechnol 1993, 38:776-783.
    • (1993) Appl Microbiol Biotechnol , vol.38 , pp. 776-783
    • Kötter, P.1    Ciriacy, M.2
  • 2
    • 0031050344 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the cysteine residues in the Pichia stipitis xylose reductase
    • 9119198
    • Zhang YY Lee H Site-directed mutagenesis of the cysteine residues in the Pichia stipitis xylose reductase FEMS Microbiol Lett 1997, 147(2):227-232. 9119198
    • (1997) FEMS Microbiol Lett , vol.147 , Issue.2 , pp. 227-232
    • Zhang, Y.Y.1    Lee, H.2
  • 3
    • 0032008240 scopus 로고    scopus 로고
    • Mutational analysis of the role of the conserved lysine-270 in the Pichia stipitis xylose reductase
    • 9485600
    • Kostrzynska M Sopher CR Lee H Mutational analysis of the role of the conserved lysine-270 in the Pichia stipitis xylose reductase FEMS Microbiol Lett 1998, 159(1):107-112. 9485600
    • (1998) FEMS Microbiol Lett , vol.159 , Issue.1 , pp. 107-112
    • Kostrzynska, M.1    Sopher, C.R.2    Lee, H.3
  • 4
    • 15544372361 scopus 로고    scopus 로고
    • Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc
    • 15623532
    • Watanabe S Kodaki T Makino K Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc J Biol Chem 2005, 280(11):10340-10349. 15623532
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 10340-10349
    • Watanabe, S.1    Kodaki, T.2    Makino, K.3
  • 6
    • 0030821699 scopus 로고    scopus 로고
    • Comparative anatomy of the aldo-keto reductase superfamily
    • 1218714 9307009
    • Jez JM Bennett MJ Schlegel BP Lewis M Penning TM Comparative anatomy of the aldo-keto reductase superfamily Biochem J 1997, 326:625-636. 1218714 9307009
    • (1997) Biochem J , vol.326 , pp. 625-636
    • Jez, J.M.1    Bennett, M.J.2    Schlegel, B.P.3    Lewis, M.4    Penning, T.M.5
  • 7
    • 0031826033 scopus 로고    scopus 로고
    • The structure and function of yeast xylose (aldose) reductases
    • 9730277
    • Lee H The structure and function of yeast xylose (aldose) reductases Yeast 1998, 14(11):977-984. 9730277
    • (1998) Yeast , vol.14 , Issue.11 , pp. 977-984
    • Lee, H.1
  • 8
    • 12844287005 scopus 로고    scopus 로고
    • The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography
    • 1134675 15320875
    • Petschacher B Leitgeb S Kavanagh KL Wilson DK Nidetzky B The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography Biochem J 2005, 385:75-83. 1134675 15320875
    • (2005) Biochem J , vol.385 , pp. 75-83
    • Petschacher, B.1    Leitgeb, S.2    Kavanagh, K.L.3    Wilson, D.K.4    Nidetzky, B.5
  • 9
    • 0042371815 scopus 로고    scopus 로고
    • Structure of xylose reductase bound to NAD(+) and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
    • 1223518 12733986
    • Kavanagh KL Klimacek M Nidetzky B Wilson DK Structure of xylose reductase bound to NAD(+) and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases Biochem J 2003, 373:319-326. 1223518 12733986
    • (2003) Biochem J , vol.373 , pp. 319-326
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 10
    • 33646473069 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes as catalysts for organic synthesis
    • SAN DIEGO, ELSEVIER ACADEMIC PRESS INC Gates B, Knözinger H
    • Reetz MT Directed evolution of enantioselective enzymes as catalysts for organic synthesis Advances in Catalysis SAN DIEGO, ELSEVIER ACADEMIC PRESS INC Gates B, Knözinger H 2006, 49:1-69.
    • (2006) Advances in Catalysis , vol.49 , pp. 1-69
    • Reetz, M.T.1
  • 11
    • 33845288649 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability
    • Reetz MT D Carballeira J Vogel A Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability Angew Chem, Int Ed 2006, 45(46):7745-7751.
    • (2006) Angew Chem, Int Ed , vol.45 , Issue.46 , pp. 7745-7751
    • Reetz, M.T.D.1    Carballeira, J.2    Vogel, A.3
  • 12
    • 33744475011 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space
    • Reetz MT Wang LW Bocola M Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space Angew Chem, Int Ed 2006, 45(8):1236-1241.
    • (2006) Angew Chem, Int Ed , vol.45 , Issue.8 , pp. 1236-1241
    • Reetz, M.T.1    Wang, L.W.2    Bocola, M.3
  • 13
    • 22144485602 scopus 로고    scopus 로고
    • Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test
    • Reetz MT Bocola M Carballeira JD Zha DX Vogel A Expanding the range of substrate acceptance of enzymes: Combinatorial active-site saturation test Angew Chem, Int Ed 2005, 44(27):4192-4196.
    • (2005) Angew Chem, Int Ed , vol.44 , Issue.27 , pp. 4192-4196
    • Reetz, M.T.1    Bocola, M.2    Carballeira, J.D.3    Zha, D.X.4    Vogel, A.5
  • 14
    • 0037118693 scopus 로고    scopus 로고
    • The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis
    • 12102621
    • Kavanagh KL Klimacek M Nidetzky B Wilson DK The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis Biochemistry 2002, 41(28):8785-8795. 12102621
    • (2002) Biochemistry , vol.41 , Issue.28 , pp. 8785-8795
    • Kavanagh, K.L.1    Klimacek, M.2    Nidetzky, B.3    Wilson, D.K.4
  • 15
    • 3142764482 scopus 로고    scopus 로고
    • Development and large scale benchmark testing of the PROSPECTOR_3 threading algorithm
    • Skolnick J Kihara D Zhang Y Development and large scale benchmark testing of the PROSPECTOR_3 threading algorithm Proteins: Struct, Funct, Bioinf 2004, 56(3):502-518.
    • (2004) Proteins: Struct, Funct, Bioinf , vol.56 , Issue.3 , pp. 502-518
    • Skolnick, J.1    Kihara, D.2    Zhang, Y.3
  • 16
    • 2442676589 scopus 로고    scopus 로고
    • Automated structure prediction of weakly homologous proteins on a genomic scale
    • 419651 15126668
    • Zhang Y Skolnick J Automated structure prediction of weakly homologous proteins on a genomic scale Proc Natl Acad Sci U S A 2004, 101(20):7594-7599. 419651 15126668
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.20 , pp. 7594-7599
    • Zhang, Y.1    Skolnick, J.2
  • 17
    • 26844452043 scopus 로고    scopus 로고
    • Engineering Candida tenuis xylose reductase for improved utilization of NADH: Antagonistic effects of multiple side chain replacements and performance of site-directed mutants under simulated in vivo conditions
    • 1265968 16204564
    • Petschacher B Nidetzky B Engineering Candida tenuis xylose reductase for improved utilization of NADH: Antagonistic effects of multiple side chain replacements and performance of site-directed mutants under simulated in vivo conditions Appl Environ Microbiol 2005, 71(10):6390-6393. 1265968 16204564
    • (2005) Appl Environ Microbiol , vol.71 , Issue.10 , pp. 6390-6393
    • Petschacher, B.1    Nidetzky, B.2
  • 18
    • 0031034657 scopus 로고    scopus 로고
    • Combinatorial manipulation of three key active site residues in glycinamide ribonucleotide transformylase
    • 9051735
    • Warren MS Benkovic SJ Combinatorial manipulation of three key active site residues in glycinamide ribonucleotide transformylase Protein Eng 1997, 10(1):63-68. 9051735
    • (1997) Protein Eng , vol.10 , Issue.1 , pp. 63-68
    • Warren, M.S.1    Benkovic, S.J.2
  • 19
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz MT Carballeira JD Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes Nat Protocols 2007, 2(4):891-903.
    • (2007) Nat Protocols , vol.2 , Issue.4 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 20
    • 0035477024 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective enzyme through combinatorial multiple-cassette mutagenesis
    • Reetz MT Wilensek S Zha DX Jaeger KE Directed evolution of an enantioselective enzyme through combinatorial multiple-cassette mutagenesis Angew Chem, Int Ed 2001, 40(19):3589-3591.
    • (2001) Angew Chem, Int Ed , vol.40 , Issue.19 , pp. 3589-3591
    • Reetz, M.T.1    Wilensek, S.2    Zha, D.X.3    Jaeger, K.E.4
  • 21
    • 34948882785 scopus 로고    scopus 로고
    • Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein-engineered NADH-preferring xylose reductase from Pichia stipitis
    • 17768247
    • Watanabe S Abu Saleh A Pack SP Annaluru N Kodaki T Makino K Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein-engineered NADH-preferring xylose reductase from Pichia stipitis Microbiology 2007, 153(9):3044-3054. 17768247
    • (2007) Microbiology , vol.153 , Issue.9 , pp. 3044-3054
    • Watanabe, S.1    Abu Saleh, A.2    Pack, S.P.3    Annaluru, N.4    Kodaki, T.5    Makino, K.6
  • 22
    • 15444371063 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa
    • 1065158 15746370
    • Woodyer R Simurdiak M van der Donk WA Zhao HM Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa Appl Environ Microbiol 2005, 71(3):1642-1647. 1065158 15746370
    • (2005) Appl Environ Microbiol , vol.71 , Issue.3 , pp. 1642-1647
    • Woodyer, R.1    Simurdiak, M.2    van der Donk, W.A.3    Zhao, H.M.4
  • 23
    • 33746891860 scopus 로고    scopus 로고
    • 2O-forming NADH oxidase and impact on redox metabolism
    • 16473032
    • 2O-forming NADH oxidase and impact on redox metabolism Metab Eng 2006, 8(4):303-314. 16473032
    • (2006) Metab Eng , vol.8 , Issue.4 , pp. 303-314
    • Heux, S.1    Cachon, R.2    Dequin, S.3
  • 24
    • 0030772483 scopus 로고    scopus 로고
    • Expression of different levels of enzymes from the Pichia stipitis XYL1 and XYL2 genes in Saccharomyces cerevisiae and its effects on product formation during xylose utilisation
    • 9299780
    • Walfridsson M Anderlund M Bao X HahnHagerdal B Expression of different levels of enzymes from the Pichia stipitis XYL1 and XYL2 genes in Saccharomyces cerevisiae and its effects on product formation during xylose utilisation Appl Microbiol Biotechnol 1997, 48(2):218-224. 9299780
    • (1997) Appl Microbiol Biotechnol , vol.48 , Issue.2 , pp. 218-224
    • Walfridsson, M.1    Anderlund, M.2    Bao, X.3    HahnHagerdal, B.4
  • 26
    • 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
    • 1756986
    • Amore R Kotter P Kuster C Ciriacy M Hollenberg CP 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 1991, 109(1):89-97. 1756986
    • (1991) Gene , vol.109 , Issue.1 , pp. 89-97
    • Amore, R.1    Kotter, P.2    Kuster, C.3    Ciriacy, M.4    Hollenberg, C.P.5
  • 27
    • 0141992693 scopus 로고    scopus 로고
    • High-throughput screens based on NAD(P)H depletion
    • Totowa, NJ, Humana Press Inc Arnold FH, Georgiou G
    • Glieder A Meinhold P High-throughput screens based on NAD(P)H depletion Directed Enzyme Evolution: Screening and Selection Methods Totowa, NJ, Humana Press Inc Arnold FH, Georgiou G 2003, 230:157-170.
    • (2003) Directed Enzyme Evolution: Screening and Selection Methods , vol.230 , pp. 157-170
    • Glieder, A.1    Meinhold, P.2
  • 28
    • 33646115667 scopus 로고    scopus 로고
    • High-throughput mutagenesis to evaluate models of stereochemical control in ketoreductase domains from the erythromycin polyketide synthase
    • 16638534
    • O'Hare HM Baerga-Ortiz A Popovic B Spencer JB Leadlay PF High-throughput mutagenesis to evaluate models of stereochemical control in ketoreductase domains from the erythromycin polyketide synthase Chem Biol 2006, 13(3):287-296. 16638534
    • (2006) Chem Biol , vol.13 , Issue.3 , pp. 287-296
    • O'Hare, H.M.1    Baerga-Ortiz, A.2    Popovic, B.3    Spencer, J.B.4    Leadlay, P.F.5
  • 32
    • 0021959310 scopus 로고
    • Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis
    • 1144764 3921014
    • Verduyn C Van Kleef R Frank J Schreuder H Van Dijken JP Scheffers WA Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis Biochem J 1985, 226(3):669-677. 1144764 3921014
    • (1985) Biochem J , vol.226 , Issue.3 , pp. 669-677
    • Verduyn, C.1    Van Kleef, R.2    Frank, J.3    Schreuder, H.4    Van Dijken, J.P.5    Scheffers, W.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.