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Volumn 87, Issue 2, 2010, Pages 571-581

Cloning and characterization of a thermostable xylitol dehydrogenase from Rhizobium etli CFN42

Author keywords

Characterization; Homology modeling; Rhizobium etli; Thermostability; Xylitol dehydrogenase

Indexed keywords

AMINO ACID RESIDUES; DENATURATION TEMPERATURES; DNA SEQUENCE ANALYSIS; GEL-FILTRATION CHROMATOGRAPHY; HALF LIVES; HEAT INACTIVATION; HOMOLOGY MODELING; HOMOTETRAMERS; OPEN READING FRAME; OPTIMUM TEMPERATURE; POLYACRYLAMIDE GELS; POLYOLS; PURIFIED ENZYME; RHIZOBIUM ETLI; SEQUENCE ANALYSIS; SODIUM DODECYL SULFATE; THERMAL STABILITY;

EID: 77953082532     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2478-6     Document Type: Article
Times cited : (18)

References (33)
  • 2
    • 34247173915 scopus 로고    scopus 로고
    • Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop
    • Annaluru N, Watanabe S, Pack SP, Saleh AA, Kodaki T, Makino K (2007) Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop. J Biotechnol 129(4):717-722
    • (2007) J Biotechnol , vol.129 , Issue.4 , pp. 717-722
    • Annaluru, N.1    Watanabe, S.2    Pack, S.P.3    Saleh, A.A.4    Kodaki, T.5    Makino, K.6
  • 3
    • 0035895426 scopus 로고    scopus 로고
    • Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 A resolution
    • Banfield MJ, Salvucci ME, Baker EN, Smith CA (2001) Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 A resolution. J Mol Biol 306 (2):239-250
    • (2001) J Mol Biol , vol.306 , Issue.2 , pp. 239-250
    • Banfield, M.J.1    Salvucci, M.E.2    Baker, E.N.3    Smith, C.A.4
  • 4
    • 21644471102 scopus 로고    scopus 로고
    • Characterization of the AXDH gene and the encoded xylitol dehydrogenase from the dimorphic yeast Arxula adeninivorans
    • Böer E, Wartmann T, Schmidt S, Bode R, Gellissen G, Kunze G (2005) Characterization of the AXDH gene and the encoded xylitol dehydrogenase from the dimorphic yeast Arxula adeninivorans. Antonie Van Leeuwenhoek 87(3):233-243
    • (2005) Antonie van Leeuwenhoek , vol.87 , Issue.3 , pp. 233-243
    • Böer, E.1    Wartmann, T.2    Schmidt, S.3    Bode, R.4    Gellissen, G.5    Kunze, G.6
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 6
    • 70450224038 scopus 로고    scopus 로고
    • ESBRI: A web server for evaluating salt bridges in proteins
    • Costantini S, Colonna G, Facchiano AM (2008) ESBRI: a web server for evaluating salt bridges in proteins. Bioinformation 3(3):137-8
    • (2008) Bioinformation , vol.3 , Issue.3 , pp. 137-138
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 7
    • 48249153490 scopus 로고    scopus 로고
    • Metal binding affinity and selectivity in metalloproteins: Insights from computational studies
    • Dudev T, Lim C (2008) Metal binding affinity and selectivity in metalloproteins: insights from computational studies. Annu Rev Biophys 37:97-116
    • (2008) Annu Rev Biophys , vol.37 , pp. 97-116
    • Dudev, T.1    Lim, C.2
  • 8
    • 33644843318 scopus 로고    scopus 로고
    • Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity
    • Ehrensberger AH, Elling RA, Wilson DK (2006) Structure-guided engineering of xylitol dehydrogenase cosubstrate specificity. Structure 14(3):567-575
    • (2006) Structure , vol.14 , Issue.3 , pp. 567-575
    • Ehrensberger, A.H.1    Elling, R.A.2    Wilson, D.K.3
  • 9
    • 0018786675 scopus 로고
    • Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase
    • Eklund H, Branden CI (1979) Structural differences between apo- and holoenzyme of horse liver alcohol dehydrogenase. J Biol Chem 254(9):3458-3461
    • (1979) J Biol Chem , vol.254 , Issue.9 , pp. 3458-3461
    • Eklund, H.1    Branden, C.I.2
  • 10
    • 46449123144 scopus 로고    scopus 로고
    • Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution
    • Goihberg E, Dym O, Tel-Or S, Shimon L, Frolow F, Peretz M, Burstein Y (2008) Thermal stabilization of the protozoan Entamoeba histolytica alcohol dehydrogenase by a single proline substitution. Proteins 72(2):711-719
    • (2008) Proteins , vol.72 , Issue.2 , pp. 711-719
    • Goihberg, E.1    Dym, O.2    Tel-Or, S.3    Shimon, L.4    Frolow, F.5    Peretz, M.6    Burstein, Y.7
  • 12
    • 33744469369 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of hyper-thermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii
    • Higashi N, Matsuura T, Nakagawa A, Ishikawa K (2005) Crystallization and preliminary X-ray analysis of hyper-thermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii. Acta Crystallogr Sect F Struct Biol Cryst Commun 61(Pt 4):432-434
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , Issue.PART 4 , pp. 432-434
    • Higashi, N.1    Matsuura, T.2    Nakagawa, A.3    Ishikawa, K.4
  • 15
    • 33845472270 scopus 로고    scopus 로고
    • Molecular cloning and characterization of NAD(+)-dependent xylitol dehydrogenase from Candida tropicalis ATCC 20913
    • Ko BS, Jung HC, Kim JH (2006) Molecular cloning and characterization of NAD(+)-dependent xylitol dehydrogenase from Candida tropicalis ATCC 20913. Biotechnol Prog 22(6):1708-1714
    • (2006) Biotechnol Prog , vol.22 , Issue.6 , pp. 1708-1714
    • Ko, B.S.1    Jung, H.C.2    Kim, J.H.3
  • 16
    • 0032557624 scopus 로고    scopus 로고
    • NADP-dependent bacterial alcohol dehydrogenases: Crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii
    • Korkhin Y, Kalb AJ, Peretz M, Bogin O, Burstein Y, Frolow F (1998) NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J Mol Biol 278(5):967-981
    • (1998) J Mol Biol , vol.278 , Issue.5 , pp. 967-981
    • Korkhin, Y.1    Kalb, A.J.2    Peretz, M.3    Bogin, O.4    Burstein, Y.5    Frolow, F.6
  • 17
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thornton JM (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26(2):283-291
    • (1993) J Appl Crystallogr , vol.26 , Issue.2 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 18
    • 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 JK, Koo BS, Kim SY (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(10):6179-6188
    • (2003) Appl Environ Microbiol , vol.69 , Issue.10 , pp. 6179-6188
    • Lee, J.K.1    Koo, B.S.2    Kim, S.Y.3
  • 19
    • 0029562477 scopus 로고
    • NAD-binding domains of dehydrogenases
    • Lesk AM (1995) NAD-binding domains of dehydrogenases. Curr Opin Struct Biol 5(6):775-783
    • (1995) Curr Opin Struct Biol , vol.5 , Issue.6 , pp. 775-783
    • Lesk, A.M.1
  • 20
    • 0032703356 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability
    • Li C, Heatwole J, Soelaiman S, Shoham M (1999) Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability. Proteins 37(4):619-627
    • (1999) Proteins , vol.37 , Issue.4 , pp. 619-627
    • Li, C.1    Heatwole, J.2    Soelaiman, S.3    Shoham, M.4
  • 21
    • 0037325074 scopus 로고    scopus 로고
    • Characterization of recombinant xylitol dehydrogenase from galactocandida mastotermitis expressed in escherichia coli
    • Nidetzky B, Helmer H, Klimacek M, Lunzer R, Mayer G (2003) Characterization of recombinant xylitol dehydrogenase from Galactocandida mastotermitis expressed in Escherichia coli. Chemico-Biological Interactions 143:533-542
    • (2003) Chemico-Biological Interactions , vol.143 , pp. 533-542
    • Nidetzky, B.1    Helmer, H.2    Klimacek, M.3    Lunzer, R.4    Mayer, G.5
  • 22
    • 0036375898 scopus 로고    scopus 로고
    • Medium-chain dehydro-genases/reductases (MDR). Family characterizations including genome comparisons and active site modeling
    • Nordling E, Jornvall H, Persson B (2002) Medium-chain dehydro-genases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-4276
    • (2002) Eur J Biochem , vol.269 , Issue.17 , pp. 4267-4276
    • Nordling, E.1    Jornvall, H.2    Persson, B.3
  • 23
    • 0036955763 scopus 로고    scopus 로고
    • Purification and characterisation of NAD+-dependent xylitol dehydrogenase from fusarium oxysporum
    • Panagiotou G, Kekos D, Macris BJ, Christakopoulos P (2002) Purification and characterisation of NAD+-dependent xylitol dehydrogenase from Fusarium oxysporum. Biotechnol Lett 24 (24):2089-2092
    • (2002) Biotechnol Lett , vol.24 , Issue.24 , pp. 2089-2092
    • Panagiotou, G.1    Kekos, D.2    Macris, B.J.3    Christakopoulos, P.4
  • 25
    • 38549142508 scopus 로고    scopus 로고
    • Polyol conversion specificity of bacillus pallidus
    • Poonperm W, Takata G, Izumori, K (2007) Polyol conversion specificity of Bacillus pallidus. Biosci Biotechnol Biochem 72(1):231-235
    • (2007) Biosci Biotechnol Biochem , vol.72 , Issue.1 , pp. 231-235
    • Poonperm, W.1    Takata, G.2    Izumori, K.3
  • 28
    • 0000978175 scopus 로고
    • Purification and properties of d-xylulose reductase from pachysolen tanno-philus
    • Shigemi M, Masako M, Kazuko A, Anthony JS (1986) Purification and properties of d-xylulose reductase from Pachysolen tanno-philus. J Ferm Technol 64(3):219-225
    • (1986) J Ferm Technol , vol.64 , Issue.3 , pp. 219-225
    • Shigemi, M.1    Masako, M.2    Kazuko, A.3    Anthony, J.S.4
  • 30
    • 3242816305 scopus 로고    scopus 로고
    • Cloning and expression of a NAD+-dependent xylitol dehydro-genase gene (xdhA) of aspergillus oryzae
    • Tran LH, Kitamoto N, Kawai K, Takamizawa K, Suzuki T (2004) Cloning and expression of a NAD+-dependent xylitol dehydro-genase gene (xdhA) of Aspergillus oryzae. J Biosci Bioeng 97 (6):419-422
    • (2004) J Biosci Bioeng , vol.97 , Issue.6 , pp. 419-422
    • Tran, L.H.1    Kitamoto, N.2    Kawai, K.3    Takamizawa, K.4    Suzuki, T.5
  • 31
    • 0242432552 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from saccharo-myces cerevisiae and rana perezi
    • Valencia E, Rosell A, Larroy C, Farres J, Biosca JA, Fita I, Pares X, Ochoa WF (2003) Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharo-myces cerevisiae and Rana perezi. Acta Crystallogr D Biol Crystallogr 59(Pt 2):334-337
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , Issue.PART 2 , pp. 334-337
    • Valencia, E.1    Rosell, A.2    Larroy, C.3    Farres, J.4    Biosca, J.A.5    Fita, I.6    Pares, X.7    Ochoa, W.F.8
  • 33
    • 15544372361 scopus 로고    scopus 로고
    • Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc
    • Watanabe S, Kodaki T, Makino K (2005) Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc. J Biol Chem 280(11):10340-10349
    • (2005) J Biol Chem , vol.280 , Issue.11 , pp. 10340-10349
    • Watanabe, S.1    Kodaki, T.2    Makino, K.3


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