메뉴 건너뛰기




Volumn 193, Issue 12, 2011, Pages 3009-3019

Characterization of a zinc-containing alcohol dehydrogenase with stereoselectivity from the hyperthermophilic archaeon Thermococcus guaymasensis

Author keywords

[No Author keywords available]

Indexed keywords

2,3 BUTANEDIOL; ACETOIN; ALCOHOL DEHYDROGENASE; KETONE; MESO 2,3 BUTANEDIOL; METHANOL; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; ZINC;

EID: 79958044337     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01433-10     Document Type: Article
Times cited : (41)

References (70)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul, S. F., et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 2
    • 0026969319 scopus 로고
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases
    • +-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases. Biochemistry. 31: 12514-12523.
    • (1992) Biochemistry , vol.31 , pp. 12514-12523
    • Ammendola, S.1
  • 3
    • 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
  • 5
    • 67651160661 scopus 로고    scopus 로고
    • Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Bashir, Q., N. Rashid, F. Jamil, T. Imanaka, and M. Akhtar. 2009. Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis. J. Biochem. 146:95-102.
    • (2009) J. Biochem. , vol.146 , pp. 95-102
    • Bashir, Q.1    Rashid, N.2    Jamil, F.3    Imanaka, T.4    Akhtar, M.5
  • 7
    • 0027480789 scopus 로고
    • Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes
    • Blomqvist, K., et al. 1993. Characterization of the genes of the 2,3-butanediol operons from Klebsiella terrigena and Enterobacter aerogenes. J. Bacteriol. 175:1392-1404.
    • (1993) J. Bacteriol. , vol.175 , pp. 1392-1404
    • Blomqvist, K.1
  • 8
    • 0036838706 scopus 로고    scopus 로고
    • Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging
    • Bogin, O., et al. 2002. Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging. Protein Sci. 11:2561-2574.
    • (2002) Protein Sci. , vol.11 , pp. 2561-2574
    • Bogin, O.1
  • 9
    • 0031837178 scopus 로고    scopus 로고
    • Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residue with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase
    • Bogin, O., et al. 1998. Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residue with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase. Protein Sci. 7:1156-1163.
    • (1998) Protein Sci. , vol.7 , pp. 1156-1163
    • Bogin, O.1
  • 10
    • 0032570486 scopus 로고    scopus 로고
    • Kinetic resolution of vic-diols by Bacillus stearothermophilus diacetyl reductase
    • Bortolini, O., et al. 1998. Kinetic resolution of vic-diols by Bacillus stearothermophilus diacetyl reductase. Tetrahedron Asymmetry. 9:647-651.
    • (1998) Tetrahedron Asymmetry , vol.9 , pp. 647-651
    • Bortolini, O.1
  • 11
    • 70349453952 scopus 로고    scopus 로고
    • Structure and function of the L-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Bowyer, A., et al. 2009. Structure and function of the L-threonine dehydrogenase (TkTDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis. J. Struct. Biol. 168:294-304.
    • (2009) J. Struct. Biol. , vol.168 , pp. 294-304
    • Bowyer, A.1
  • 12
    • 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
  • 13
    • 0014603264 scopus 로고
    • Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups
    • Bühner, M., and H. Sund. 1969. Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups. Eur. J. Biochem. 11:73-79.
    • (1969) Eur. J. Biochem. , vol.11 , pp. 73-79
    • Bühner, M.1    Sund, H.2
  • 14
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau, C., and J. M. Claverie. 2000. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 275:32383-32386.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 15
    • 0031753314 scopus 로고    scopus 로고
    • Thermococcus guaymasensis sp. nov. and Thermococcus aggregans sp. nov., two novel thermophilic archaea isolated from the Guaymas Basin hydrothermal vent site
    • Canganella, F., W. J. Jones, A. Gambacorta, and G. Antranikian. 1998. Thermococcus guaymasensis sp. nov. and Thermococcus aggregans sp. nov., two novel thermophilic archaea isolated from the Guaymas Basin hydrothermal vent site. Int. J. Syst. Bacteriol. 48:1181-1185.
    • (1998) Int. J. Syst. Bacteriol. , vol.48 , pp. 1181-1185
    • Canganella, F.1    Jones, W.J.2    Gambacorta, A.3    Antranikian, G.4
  • 16
    • 33847123483 scopus 로고    scopus 로고
    • Translational and transcriptional analysis of Sulfolobus solfataricus P2 to provide insights into alcohol and ketone utilization
    • Chong, P. K., A. M. Burja, H. Radianingtyas, A. Fazeli, and P. C. Wright. 2007. Translational and transcriptional analysis of Sulfolobus solfataricus P2 to provide insights into alcohol and ketone utilization. Proteomics. 7:424-435.
    • (2007) Proteomics , vol.7 , pp. 424-435
    • Chong, P.K.1    Burja, A.M.2    Radianingtyas, H.3    Fazeli, A.4    Wright, P.C.5
  • 17
    • 79958023358 scopus 로고    scopus 로고
    • Delano, W. L. 2002. The PyMOL molecular graphics system. Delano Scientific, Palo Alto, CA.
    • (2002)
    • Delano, W.L.1
  • 18
    • 24944463449 scopus 로고    scopus 로고
    • Posttranslational protein modification in Archaea
    • Eichler, J., and M. W. W. Adams. 2005. Posttranslational protein modification in Archaea. Microbiol. Mol. Biol. Rev. 69:393-425.
    • (2005) Microbiol. Mol. Biol. Rev. , vol.69 , pp. 393-425
    • Eichler, J.1    Adams, M.W.W.2
  • 19
    • 0037468609 scopus 로고    scopus 로고
    • Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity
    • Esposito, L., et al. 2003. Structural study of a single-point mutant of Sulfolobus solfataricus alcohol dehydrogenase with enhanced activity. FEBS Lett. 539:14-18.
    • (2003) FEBS Lett , vol.539 , pp. 14-18
    • Esposito, L.1
  • 20
    • 0036301867 scopus 로고    scopus 로고
    • Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution
    • Esposito, L., et al. 2002. Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution. J. Mol. Biol. 318:463-477.
    • (2002) J. Mol. Biol. , vol.318 , pp. 463-477
    • Esposito, L.1
  • 21
    • 13544250517 scopus 로고    scopus 로고
    • Complete genome sequence of the hyperthermophilic archaeon Thermocococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes
    • Fukui, T., et al. 2005. Complete genome sequence of the hyperthermophilic archaeon Thermocococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res. 15:352-363.
    • (2005) Genome Res , vol.15 , pp. 352-363
    • Fukui, T.1
  • 22
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy Server
    • J. M. Walker (ed.), Humana Press, Totowa, NJ
    • Gasteiger, E., et al. 2005. Protein identification and analysis tools on the ExPASy Server, p. 571-607. In J. M. Walker (ed.), The proteomics protocols handbook. Humana Press, Totowa, NJ.
    • (2005) The proteomics protocols handbook , pp. 571-607
    • Gasteiger, E.1
  • 23
    • 33845679397 scopus 로고    scopus 로고
    • A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase
    • Goihberg, E., et al. 2007. A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase. Proteins. 66:196-204.
    • (2007) Proteins , vol.66 , pp. 196-204
    • Goihberg, E.1
  • 24
    • 0034680769 scopus 로고    scopus 로고
    • Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product
    • González, E., et al. 2000. Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. J. Biol. Chem. 275:35876-35885.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35876-35885
    • González, E.1
  • 25
    • 0043123405 scopus 로고    scopus 로고
    • The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
    • Guy, J. E., M. N. Isupov, and J. A. Littlechild. 2003. The structure of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix. J. Mol. Biol. 331:1041-1051.
    • (2003) J. Mol. Biol. , vol.331 , pp. 1041-1051
    • Guy, J.E.1    Isupov, M.N.2    Littlechild, J.A.3
  • 26
    • 17044438727 scopus 로고    scopus 로고
    • Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii
    • Higashi, N., H. Fukada, and K. Ishikawa. 2005. Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii. J. Biosci. Bioeng. 99:175-180.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 175-180
    • Higashi, N.1    Fukada, H.2    Ishikawa, K.3
  • 27
    • 33744469369 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii
    • Higashi, N., T. Matsuura, A. Nakagawa, and K. Ishikawa. 2005. Crystallization and preliminary X-ray analysis of hyperthermophilic L-threonine dehydrogenase from the archaeon Pyrococcus horikoshii. Acta Crystallogr. F 61:432-434.
    • (2005) Acta Crystallogr. F , vol.61 , pp. 432-434
    • Higashi, N.1    Matsuura, T.2    Nakagawa, A.3    Ishikawa, K.4
  • 28
    • 1842451878 scopus 로고    scopus 로고
    • Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1
    • Hirakawa, H., N. Kamiya, Y. Kawarabayashi, and T. Nagamune. 2004. Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1. J. Biosci. Bioeng. 97:202-206.
    • (2004) J. Biosci. Bioeng. , vol.97 , pp. 202-206
    • Hirakawa, H.1    Kamiya, N.2    Kawarabayashi, Y.3    Nagamune, T.4
  • 29
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel, P. H., J. M. Schmitter, P. Dessen, G. Fayat, and S. Blanquet. 1989. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. U. S. A. 86:8247-8251.
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, J.M.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 31
    • 34249071422 scopus 로고    scopus 로고
    • Anaerobic biotechnological approaches for production of liquid energy carriers from biomass
    • Karakashev, D., A. B. Thomsen, and I. Angelidaki. 2007. Anaerobic biotechnological approaches for production of liquid energy carriers from biomass. Biotechnol. Lett. 29:1005-1012.
    • (2007) Biotechnol. Lett. , vol.29 , pp. 1005-1012
    • Karakashev, D.1    Thomsen, A.B.2    Angelidaki, I.3
  • 33
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • Kopp, J., and T. Schwede. 2004. The SWISS-MODEL repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32:D230-D234.
    • (2004) Nucleic Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 34
    • 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., et al. 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. 278:967-981.
    • (1998) J. Mol. Biol. , vol.278 , pp. 967-981
    • Korkhin, Y.1
  • 35
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., C. J. Tsai, and P. Nussinov. 2000. Factors enhancing protein thermostability. Protein Eng. 13:179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, P.3
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0036182468 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction
    • Larroy, C., M. R. Fernández, E. González, X. Parés, and J. A. J. A. Biosca. 2002. Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction. Biochem. J. 361:163-172.
    • (2002) Biochem. J. , vol.361 , pp. 163-172
    • Larroy, C.1    Fernández, M.R.2    González, E.3    Parés, X.4    Biosca, J.A.J.A.5
  • 38
    • 55549124188 scopus 로고    scopus 로고
    • The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophilic and carboxydotrophic metabolism
    • Lee, H. S., et al. 2008. The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophilic and carboxydotrophic metabolism. J. Bacteriol. 190:7491-7499.
    • (2008) J. Bacteriol. , vol.190 , pp. 7491-7499
    • Lee, H.S.1
  • 39
    • 0030878620 scopus 로고    scopus 로고
    • Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain AN1
    • Li, D., and K. J. Stevenson. 1997. Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain AN1. J. Bacteriol. 179:4433-4437.
    • (1997) J. Bacteriol. , vol.179 , pp. 4433-4437
    • Li, D.1    Stevenson, K.J.2
  • 40
    • 0027945387 scopus 로고
    • Sulfide dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur
    • Ma, K., and M. W. W. Adams. 1994. Sulfide dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus: a new multifunctional enzyme involved in the reduction of elemental sulfur. J. Bacteriol. 176:6509-6517.
    • (1994) J. Bacteriol. , vol.176 , pp. 6509-6517
    • Ma, K.1    Adams, M.W.W.2
  • 41
    • 0030932016 scopus 로고    scopus 로고
    • Pyruvate ferrodoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase
    • Ma, K., A. Hutchins, S. J. S. Sung, and M. W. W. Adams. 1997. Pyruvate ferrodoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Proc. Natl. Acad. Sci. U. S. A. 94:9608-9613.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9608-9613
    • Ma, K.1    Hutchins, A.2    Sung, S.J.S.3    Adams, M.W.W.4
  • 42
    • 0029088810 scopus 로고
    • Effects of elemental sulfur on the metabolism of the deep-sea hyperthermophilic archaeon Thermococcus strain ES-1: characterization of a sulfur-regulated, non-heme iron alcohol dehydrogenase
    • Ma, K., H. Loessner, J. Heider, M. K. Johnson, and M. W. W. Adams. 1995. Effects of elemental sulfur on the metabolism of the deep-sea hyperthermophilic archaeon Thermococcus strain ES-1: characterization of a sulfur-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    Johnson, M.K.4    Adams, M.W.W.5
  • 43
    • 0028069713 scopus 로고
    • +-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
    • +-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis. Appl. Environ. Microbiol. 60:562-568.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 562-568
    • Ma, K.1    Robb, F.T.2    Adams, M.W.W.3
  • 44
    • 33644855821 scopus 로고    scopus 로고
    • Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily
    • Machielsen, R., A. R. Uria, S. W. M. Kengen, and J. van der Oost. 2006. Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily. Appl. Environ. Microbiol. 72:233-238.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 233-238
    • Machielsen, R.1    Uria, A.R.2    Kengen, S.W.M.3    van der Oost, J.4
  • 45
    • 33745272829 scopus 로고    scopus 로고
    • Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Machielsen, R., and J. van der Oost. 2006. Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. FEBS J. 273:2722-2729.
    • (2006) FEBS J. , vol.273 , pp. 2722-2729
    • Machielsen, R.1    van der, J.2
  • 46
    • 38949147846 scopus 로고    scopus 로고
    • Clusters of orthologous genes for 41 archaeal genomes and implications for evolutionary genomics of archaea
    • Makarova, K. S., A. V. Sorokin, P. S. Novichkov, U. I. Wolf, and E. V. Koonin. 2007. Clusters of orthologous genes for 41 archaeal genomes and implications for evolutionary genomics of archaea. Biol. Direct. 2:33.
    • (2007) Biol. Direct. , vol.2 , pp. 33
    • Makarova, K.S.1    Sorokin, A.V.2    Novichkov, P.S.3    Wolf, U.I.4    Koonin, E.V.5
  • 48
    • 0028927080 scopus 로고
    • Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund, S., and M. W. W. Adams. 1995. Glyceraldehyde-3-phosphate ferredoxin oxidoreductase, a novel tungsten-containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus. J. Biol. Chem. 270:8389-8392.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8389-8392
    • Mukund, S.1    Adams, M.W.W.2
  • 49
    • 34447520336 scopus 로고    scopus 로고
    • Biocatalytic racemization of synthetically important functionalized α-hydroxyketones using microbial cells
    • Nestl, B. M., et al. 2007. Biocatalytic racemization of synthetically important functionalized α-hydroxyketones using microbial cells. Tetrahedron Asymmetry. 18:1465-1474.
    • (2007) Tetrahedron Asymmetry , vol.18 , pp. 1465-1474
    • Nestl, B.M.1
  • 50
    • 34547263921 scopus 로고    scopus 로고
    • Thermococcus thioreducens sp. nov., a novel hyperthermophilic, obligately sulfur-reducing archaeon from a deep-sea hydrothermal vent
    • Pikuta, E. V., et al. 2007. Thermococcus thioreducens sp. nov., a novel hyperthermophilic, obligately sulfur-reducing archaeon from a deep-sea hydrothermal vent. Int. J. Syst. Evol. Microbiol. 57:1612-1618.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 1612-1618
    • Pikuta, E.V.1
  • 51
    • 84913063444 scopus 로고
    • Specification of the stereospecificity of some oxido-reductases by diamond lattice sections
    • Prelog, V. 1964. Specification of the stereospecificity of some oxido-reductases by diamond lattice sections. Pure Appl. Chem. 9:119-130.
    • (1964) Pure Appl. Chem. , vol.9 , pp. 119-130
    • Prelog, V.1
  • 52
    • 0035078281 scopus 로고    scopus 로고
    • Alcohol dehydrogenase from Sulfolobus solfataricus
    • Raia, C. A., A. Giordano, and M. Rossi. 2001. Alcohol dehydrogenase from Sulfolobus solfataricus. Methods Enzymol. 331:176-195.
    • (2001) Methods Enzymol. , vol.331 , pp. 176-195
    • Raia, C.A.1    Giordano, A.2    Rossi, M.3
  • 53
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • Reid, M. F., and C. A. Fewson. 1994. Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol. 20:13-56.
    • (1994) Crit. Rev. Microbiol. , vol.20 , pp. 13-56
    • Reid, M.F.1    Fewson, C.A.2
  • 54
    • 0024296509 scopus 로고
    • Transcription termination in the archaebacterium Sulfolobus: signal structures and linkage to transcription initiation
    • Reiter, W. D., P. Palm, and W. Zillig. 1988. Transcription termination in the archaebacterium Sulfolobus: signal structures and linkage to transcription initiation. Nucleic Acids Res. 16:2445-2459.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2445-2459
    • Reiter, W.D.1    Palm, P.2    Zillig, W.3
  • 55
    • 0023656081 scopus 로고
    • +-dependent alcohol dehydrogenase: purification and properties
    • +-dependent alcohol dehydrogenase: purification and properties. Eur. J. Biochem. 167:475-479.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 475-479
    • Rella, R.1
  • 56
    • 34347361558 scopus 로고    scopus 로고
    • Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins
    • Saelensminde, G., Ø. Halskau, R. Helland, N. P. Willassen, and I. Jonassen. 2007. Structure-dependent relationships between growth temperature of prokaryotes and the amino acid frequency in their proteins. Extremophiles. 11:585-596.
    • (2007) Extremophiles , vol.11 , pp. 585-596
    • Saelensminde, G.1    Halskau, Ø.2    Helland, R.3    Willassen, N.P.4    Jonassen, I.5
  • 58
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31:3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 59
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga
    • Selig, M., K. B. Xavier, H. Santos, and P. Schönheit. 1997. Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch. Microbiol. 167:217-232.
    • (1997) Arch. Microbiol. , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schönheit, P.4
  • 60
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68:850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 61
    • 9744254931 scopus 로고    scopus 로고
    • The first evidence of anaerobic CO oxidation coupled with H2 production by a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent
    • Sokolova, T. G., et al. 2004. The first evidence of anaerobic CO oxidation coupled with H2 production by a hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent. Extremophiles. 8:317-323.
    • (2004) Extremophiles , vol.8 , pp. 317-323
    • Sokolova, T.G.1
  • 62
    • 77953638141 scopus 로고    scopus 로고
    • Characterization of a thermostable shortchain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus
    • Stekhanova, T. N., et al. 2010. Characterization of a thermostable shortchain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus. Appl. Environ. Microbiol. 76:4096-4098.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4096-4098
    • Stekhanova, T.N.1
  • 64
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 65
    • 0023787609 scopus 로고
    • A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences
    • Triglia, T., M. Peterson, and D. Kemp. 1988. A procedure for in vitro amplification of DNA segments that lie outside the boundaries of known sequences. Nucleic Acids Res. 16:8186.
    • (1988) Nucleic Acids Res , vol.16 , pp. 8186
    • Triglia, T.1    Peterson, M.2    Kemp, D.3
  • 66
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability
    • Vieille, C., and G. J. Zeikus. 2001. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65:1-43.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 67
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright, H. T. 1991. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26:1-52.
    • (1991) Crit. Rev. Biochem. Mol. Biol. , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 68
    • 0025144306 scopus 로고
    • Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592
    • Yan, R., and J. Chen. 1990. Coenzyme A-acylating aldehyde dehydrogenase from Clostridium beijerinckii NRRL B592. Appl. Environ. Microbiol. 56: 2591-2599.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 2591-2599
    • Yan, R.1    Chen, J.2
  • 69
    • 0026746253 scopus 로고
    • Asymmetric reduction of ketoesters with alcohol dehydrogenase from Thermoanaerobacter ethanolicus
    • Zheng, C. S., V. T. Pham, R. S. Phillips. 1992. Asymmetric reduction of ketoesters with alcohol dehydrogenase from Thermoanaerobacter ethanolicus. Bio. Med. Chem. Lett. 2:619-622.
    • (1992) Bio. Med. Chem. Lett. , vol.2 , pp. 619-622
    • Zheng, C.S.1    Pham, V.T.2    Phillips, R.S.3
  • 70
    • 33845205018 scopus 로고    scopus 로고
    • Asymmetric ketone reduction by a hyperthermophilic alcohol dehydrogenase: the substrate specificity, enantioselectivity and tolerance of organic solvents
    • Zhu, D., H. T. Malik, and L. Hua. 2006. Asymmetric ketone reduction by a hyperthermophilic alcohol dehydrogenase: the substrate specificity, enantioselectivity and tolerance of organic solvents. Tetrahedron Asymmetry. 17: 3010-3014.
    • (2006) Tetrahedron Asymmetry , vol.17 , pp. 3010-3014
    • Zhu, D.1    Malik, H.T.2    Hua, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.