메뉴 건너뛰기




Volumn 13, Issue 5, 2003, Pages 738-744

Overexpression, purification, and biochemical characterization of the thermostable NAD-dependent alcohol dehydrogenase from Bacillus stearothermophilus

Author keywords

Alcohol dehydrogenase; Bacillus stearothermophilus; Enzymatic characterization; Overexpression in E. coli; Recombinant enzyme; Simple purification; Thermal resistance; Thermophilic bacterium

Indexed keywords

ALCOHOL DEHYDROGENASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; THROMBIN;

EID: 0242636174     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 0033568692 scopus 로고    scopus 로고
    • Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis
    • Antoine, E., J. L. Rolland, J. P. Raffin, and J. Dietrich. 1999. Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis. Eur. J. Biochem. 264: 880-889.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 880-889
    • Antoine, E.1    Rolland, J.L.2    Raffin, J.P.3    Dietrich, J.4
  • 2
    • 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
  • 3
    • 77956937817 scopus 로고
    • Boyer, P. D. (ed.), 3rd ed, Academic Press, New York, U.S.A
    • Brändén, C.-I., H. Jörnvall, H. Eklund, and B. Furugren. 1975. In Boyer, P. D. (ed.), The Enzymes, 3rd ed, vol. 11, pp. 103-190. Academic Press, New York, U.S.A.
    • (1975) The Enzymes , vol.11 , pp. 103-190
    • Brändén, C.-I.1    Jörnvall, H.2    Eklund, H.3    Furugren, B.4
  • 4
    • 0000084946 scopus 로고
    • Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus
    • Bryant, F. O., J. Wiegel, and L. G. Ljungdahl. 1988. Purification and properties of primary and secondary alcohol dehydrogenases from Thermoanaerobacter ethanolicus. Appl. Environ. Microbiol. 54: 460-465.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 460-465
    • Bryant, F.O.1    Wiegel, J.2    Ljungdahl, L.G.3
  • 5
    • 0028074589 scopus 로고
    • Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenases (2 degrees ADH) as a bifunctional alcohol dehydrogenase - acetyl-CoA reductive thioesterase
    • Burdette, D. and J. G. Zeikus. 1994. Purification of acetaldehyde dehydrogenase and alcohol dehydrogenases from Thermoanaerobacter ethanolicus 39E and characterization of the secondary-alcohol dehydrogenases (2 degrees ADH) as a bifunctional alcohol dehydrogenase - acetyl-CoA reductive thioesterase. Biochem. J. 302: 163-170.
    • (1994) Biochem. J. , vol.302 , pp. 163-170
    • Burdette, D.1    Zeikus, J.G.2
  • 6
    • 0030046289 scopus 로고    scopus 로고
    • Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species
    • Cannio, R., G. Fiorentino, P. Carpinelli, M. Rossi, and S. Bartolucci. 1996. Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species. J. Bacteriol. 178: 301-305.
    • (1996) J. Bacteriol. , vol.178 , pp. 301-305
    • Cannio, R.1    Fiorentino, G.2    Carpinelli, P.3    Rossi, M.4    Bartolucci, S.5
  • 7
    • 0026733875 scopus 로고
    • Danson, M. J., Hough, D. W. and Lunt, G. G. (eds.), Biochemical Society Symposium, Portland Press, London, U.K
    • Cowan, D. A. 1992. In Danson, M. J., Hough, D. W. and Lunt, G. G. (eds.), The Archaebacteria: Biochemistry and Biotechnology, Biochemical Society Symposium, 58: 149-169, Portland Press, London, U.K.
    • (1992) The Archaebacteria: Biochemistry and Biotechnology , vol.58 , pp. 149-169
    • Cowan, D.A.1
  • 8
    • 0019726115 scopus 로고
    • Partial purification and characterization of an alcohol dehydrogenase of Mycobacterium tuberculosis var. bovis (BCG)
    • De Bruyn, J., A. Johannes, M. Weckx, and M. P. Beumer-Jochmans. 1981. Partial purification and characterization of an alcohol dehydrogenase of Mycobacterium tuberculosis var. bovis (BCG). J. Gen. Microbiol. 124: 359-363.
    • (1981) J. Gen. Microbiol. , vol.124 , pp. 359-363
    • De Bruyn, J.1    Johannes, A.2    Weckx, M.3    Beumer-Jochmans, M.P.4
  • 9
    • 0242699963 scopus 로고
    • A highly resistant thermophilic organism
    • Donk, P. J. 1920. A highly resistant thermophilic organism. J. Bacteriol. 5: 373.
    • (1920) J. Bacteriol. , vol.5 , pp. 373
    • Donk, P.J.1
  • 11
    • 0030052553 scopus 로고    scopus 로고
    • Purification and characterization of the alcohol dehydrogenase from a novel strain of Bacillus stearothermophilus growing at 70°C
    • Guagliardi, A., M. Martino, I. Iaccarino, M. De Rosa, M. Rosssi, and S. Bartolucci. 1996. Purification and characterization of the alcohol dehydrogenase from a novel strain of Bacillus stearothermophilus growing at 70°C. Int. J. Biochem. Cell Biol. 28: 239-246.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 239-246
    • Guagliardi, A.1    Martino, M.2    Iaccarino, I.3    De Rosa, M.4    Rosssi, M.5    Bartolucci, S.6
  • 12
    • 0027288792 scopus 로고
    • Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas
    • Hensgens, C. M., J. Vonck, J. Van Beeumen, E. F. Van Bruggen, and T. A. Hansen. 1993. Purification and characterization of an oxygen-labile, NAD-dependent alcohol dehydrogenase from Desulfovibrio gigas. J. Bacteriol. 175: 2859-2863.
    • (1993) J. Bacteriol. , vol.175 , pp. 2859-2863
    • Hensgens, C.M.1    Vonck, J.2    Van Beeumen, J.3    Van Bruggen, E.F.4    Hansen, T.A.5
  • 13
    • 85005697480 scopus 로고
    • Dehydrogenases for the synthesis of chiral compounds
    • Hummel, W. and M. R. Kula. 1989. Dehydrogenases for the synthesis of chiral compounds. Eur. J. Biochem. 184: 1-13.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 1-13
    • Hummel, W.1    Kula, M.R.2
  • 14
    • 0027317888 scopus 로고
    • Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii
    • Ismaiel, A. A., C. X. Zhu, G. D. Colby, and J. S. Chen. 1993. Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. J. Bacteriol. 175: 5097-5105.
    • (1993) J. Bacteriol. , vol.175 , pp. 5097-5105
    • Ismaiel, A.A.1    Zhu, C.X.2    Colby, G.D.3    Chen, J.S.4
  • 15
    • 0001230359 scopus 로고
    • Thermostable enzymes in organic synthesis. 2. Asymmetric production of ketones with alcohol dehydrogenase from Thermoanaerobium brockii
    • Keinan, E., E. K. Hafeli, K. K. Seth, and R. Lamed. 1986. Thermostable enzymes in organic synthesis. 2. Asymmetric production of ketones with alcohol dehydrogenase from Thermoanaerobium brockii. J. Am. Chem. Soc. 108: 162-169.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 162-169
    • Keinan, E.1    Hafeli, E.K.2    Seth, K.K.3    Lamed, R.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structual proteins during the assembly of the head of bcteriophage T4
    • Laemmil, U. K. 1970. Cleavage of structual proteins during the assembly of the head of bcteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmil, U.K.1
  • 17
    • 0030878620 scopus 로고    scopus 로고
    • Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain ANI
    • Li, D. and J. Stevenson. 1997. Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain ANI. J. Bacteriol. 179: 4433-4437.
    • (1997) J. Bacteriol. , vol.179 , pp. 4433-4437
    • Li, D.1    Stevenson, J.2
  • 18
    • 0029829252 scopus 로고    scopus 로고
    • Purification and characterization of an alcohol dehydrogenase from Lithospermum erythrorhizon cell cultures
    • Li, S. M., Z. X. Wang, and L. Heide. 1996. Purification and characterization of an alcohol dehydrogenase from Lithospermum erythrorhizon cell cultures. Plant Cell Reports 15: 786-790.
    • (1996) Plant Cell Reports , vol.15 , pp. 786-790
    • Li, S.M.1    Wang, Z.X.2    Heide, L.3
  • 19
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • Lineweaver, H. and D. Burk. 1934. The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56: 658-666.
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 20
    • 0018749938 scopus 로고
    • Quantitative correlation of ethanol elimination rates in vivo with liver alcohol dehydrogenase activities in fed, fasted and food-restricted rats
    • Lumeng, L., W. F. Bosron, and T. K. Li. 1979. Quantitative correlation of ethanol elimination rates in vivo with liver alcohol dehydrogenase activities in fed, fasted and food-restricted rats. Biochem. Pharmacol. 28: 1547-1551.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 1547-1551
    • Lumeng, L.1    Bosron, W.F.2    Li, T.K.3
  • 21
    • 0029088810 scopus 로고
    • Effects of elemental sulfur on the metabolism of the deep-sea hyperthermophilic Archaeon Thermococcus Strain ES1: Characterization of a sufur-regulated, non-heme iron alcohol-dehydrogenase
    • Ma, K., H. Loessner, J. Heider, M. K. Jonson, and M. W. W. Adams. 1995. Effects of elemental sulfur on the metabolism of the deep-sea hyperthermophilic Archaeon Thermococcus Strain ES1: Characterization of a sufur-regulated, non-heme iron alcohol-dehydrogenase. J. Bacteriol. 177: 4748-4756.
    • (1995) J. Bacteriol. , vol.177 , pp. 4748-4756
    • Ma, K.1    Loessner, H.2    Heider, J.3    Jonson, M.K.4    Adams, M.W.W.5
  • 22
    • 0037002851 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of xylanase from fungus Trichoderma strain SY
    • Min, S. Y., B. G. Kim, C. Lee, H. G. Hur, and J. H. Ahn. 2002. Purification, characterization, and cDNA cloning of xylanase from fungus Trichoderma strain SY. J. Microbiol. Biotechnol. 12: 890-894.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 890-894
    • Min, S.Y.1    Kim, B.G.2    Lee, C.3    Hur, H.G.4    Ahn, J.H.5
  • 23
    • 0023039990 scopus 로고
    • The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterization and physiological roles
    • Neale, A. D., R. K. Scopes, J. M. Kelly, and R. E. H. Wettenhall. 1986. The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterization and physiological roles. Eur. J. Biochem. 154: 119-124.
    • (1986) Eur. J. Biochem. , vol.154 , pp. 119-124
    • Neale, A.D.1    Scopes, R.K.2    Kelly, J.M.3    Wettenhall, R.E.H.4
  • 24
    • 0017806162 scopus 로고
    • Purification and characterization of a secondary alcohol dehydrogenase from a Pseudomonad
    • Niehaus, W. G., T. Frielle, and E. A. Kingsley. 1978. Purification and characterization of a secondary alcohol dehydrogenase from a Pseudomonad. J. Bacteriol. 134: 177-183.
    • (1978) J. Bacteriol. , vol.134 , pp. 177-183
    • Niehaus, W.G.1    Frielle, T.2    Kingsley, E.A.3
  • 25
    • 0036998350 scopus 로고    scopus 로고
    • Simple purification of Shiga toxin B chain from recombinant Escherichia coli
    • Oh, Y. P., S. T. Jeong, D. W. Kim, E. C. Kim, and K. H. Yoon. 2002. Simple purification of Shiga toxin B chain from recombinant Escherichia coli. J. Microbiol. Biotechnol. 12: 986-988.
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 986-988
    • Oh, Y.P.1    Jeong, S.T.2    Kim, D.W.3    Kim, E.C.4    Yoon, K.H.5
  • 26
    • 0029141457 scopus 로고
    • Purification and kinetic properties of alcohol dehydrogenase from yellow yam tubers (Dioscorea cayenensis)
    • Oluoha, U. 1995. Purification and kinetic properties of alcohol dehydrogenase from yellow yam tubers (Dioscorea cayenensis). Plant Science 107: 1-7.
    • (1995) Plant Science , vol.107 , pp. 1-7
    • Oluoha, U.1
  • 27
    • 0024327951 scopus 로고
    • Amino acid sequence of alcohol dehydrogenase from thermophillic bacterium Thermoanaerobium brockii
    • Perez, M. and Y. Burstein. 1989. Amino acid sequence of alcohol dehydrogenase from thermophillic bacterium Thermoanaerobium brockii. Biochemistry 28: 6549-6555.
    • (1989) Biochemistry , vol.28 , pp. 6549-6555
    • Perez, M.1    Burstein, Y.2
  • 28
    • 0024989102 scopus 로고
    • Effects of substrate and temperature on the stereospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus
    • Pham, V. T. and R. S. Phillips. 1990. Effects of substrate and temperature on the stereospecificity of secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus. J. Am. Chem. Soc. 112: 3629-3632.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3629-3632
    • Pham, V.T.1    Phillips, R.S.2
  • 30
    • 0002437098 scopus 로고
    • Amplification of genomic DNA
    • M. A. Innis, D. A. Gelfand, J. J. Sninski and T. J. White (eds.), Academic Press, Inc., San Diego, CA, U.S.A
    • Saiki, R. K. 1990. Amplification of genomic DNA, pp. 13-20. In M. A. Innis, D. A. Gelfand, J. J. Sninski and T. J. White (eds.), PCR Protocols. A Guide to Methods and Applications. Academic Press, Inc., San Diego, CA, U.S.A.
    • (1990) PCR Protocols. A Guide to Methods and Applications , pp. 13-20
    • Saiki, R.K.1
  • 32
    • 0026548444 scopus 로고
    • Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and retional shift of the optimum pH
    • Sakoda, H. and T. Imanaka. 1992. Cloning and sequencing of the gene coding for alcohol dehydrogenase of Bacillus stearothermophilus and retional shift of the optimum pH. J. Bacteriol. 174: 1397-1402.
    • (1992) J. Bacteriol. , vol.174 , pp. 1397-1402
    • Sakoda, H.1    Imanaka, T.2
  • 33
    • 0023907411 scopus 로고
    • A new alcohol dehydrogenase, reactive towards methanol, from Bacillus stearothermophilus
    • Sheehan, M. C., C. J. Bailey, B. C. A. Dowds, and D. J. Mcconnell. 1988. A new alcohol dehydrogenase, reactive towards methanol, from Bacillus stearothermophilus. Biochem. J. 252: 661-666.
    • (1988) Biochem. J. , vol.252 , pp. 661-666
    • Sheehan, M.C.1    Bailey, C.J.2    Dowds, B.C.A.3    Mcconnell, D.J.4
  • 34
    • 0009460086 scopus 로고
    • Alcohol dehydrogenase, aldehyde dehydrogenase
    • Takenoshita, R. and T. Togi. 1989. Alcohol dehydrogenase, aldehyde dehydrogenase. Shin Seikagaku Jikken Tokyo 1: 269-285.
    • (1989) Shin Seikagaku Jikken Tokyo , vol.1 , pp. 269-285
    • Takenoshita, R.1    Togi, T.2
  • 35
    • 0032103265 scopus 로고    scopus 로고
    • Purification and characterization of an alcohol dehydrogenase from the Antarctic psychophile Mofaxella sp. TAE123
    • Tsigos, I., K. Velonia, I. Smonou, and V. Bouriotis. 1998. Purification and characterization of an alcohol dehydrogenase from the Antarctic psychophile Mofaxella sp. TAE123. Eur. J. Biochem. 254: 356-362.
    • (1998) Eur. J. Biochem. , vol.254 , pp. 356-362
    • Tsigos, I.1    Velonia, K.2    Smonou, I.3    Bouriotis, V.4
  • 36
    • 0035988691 scopus 로고    scopus 로고
    • The highly stable alcohol dehydrogenase of Thermomicrobium roseum: Purification and molecular characterization
    • Yoon, S.-Y., H.-S. Noh, E.-H. Kim, and K.-H. Kong. 2002. The highly stable alcohol dehydrogenase of Thermomicrobium roseum: Purification and molecular characterization. Comp. Biochem. Physiol. 132: 415-422.
    • (2002) Comp. Biochem. Physiol. , vol.132 , pp. 415-422
    • Yoon, S.-Y.1    Noh, H.-S.2    Kim, E.-H.3    Kong, K.-H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.