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Volumn 181, Issue 4, 1999, Pages 1163-1170

An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE; IRON; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; ZINC;

EID: 0032988361     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.4.1163-1170.1999     Document Type: Article
Times cited : (45)

References (72)
  • 1
    • 0028072338 scopus 로고
    • Biochemical diversity among sulfur-dependent hyperthermophilic microorganisms
    • Adams, M. W. W. 1994. Biochemical diversity among sulfur-dependent hyperthermophilic microorganisms. FEMS Microbiol. Rev. 15:267-277.
    • (1994) FEMS Microbiol. Rev. , vol.15 , pp. 267-277
    • Adams, M.W.W.1
  • 2
    • 0026969319 scopus 로고
    • Thermostable NAD-dependent alcohol dehydrogenase from Sulfolobus solfataricus: Gene and protein sequence determination and relationship to other alcohol dehydrogenases
    • Ammendola, S., C. A. Raia, C. Caruso, L. Camardella, S. D'Auria, M. De Rosa, and M. Rossi. 1992. Thermostable NAD-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    Raia, C.A.2    Caruso, C.3    Camardella, L.4    D'Auria, S.5    De Rosa, M.6    Rossi, M.7
  • 3
    • 0022270779 scopus 로고
    • 17O-water and nitric oxide binding by protocatechuate 4,5 dioxygenase and catechol 2,3 dioxygenase
    • 17O-water and nitric oxide binding by protocatechuate 4,5 dioxygenase and catechol 2,3 dioxygenase. J. Biol. Chem. 260:14035-14044.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14035-14044
    • Arciero, D.M.1    Orville, A.M.2    Lipscomb, J.D.3
  • 4
    • 0024805513 scopus 로고
    • Iron-activated alcohol dehydrogenase from Zymomonas mobilis: Spectroscopic and magnetic properties
    • Bakshi, E. N., P. Tse, K. S. Murray, G. R. Hanson, R. K. Scopes, and A. G. Wedd. 1989. Iron-activated alcohol dehydrogenase from Zymomonas mobilis: spectroscopic and magnetic properties. J. Am. Chem. Soc. 189:8707-8713.
    • (1989) J. Am. Chem. Soc. , vol.189 , pp. 8707-8713
    • Bakshi, E.N.1    Tse, P.2    Murray, K.S.3    Hanson, G.R.4    Scopes, R.K.5    Wedd, A.G.6
  • 5
    • 0020050588 scopus 로고
    • The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase I
    • Bennetzen, J. L., and B. D. Hall. 1982. The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase I. J. Biol. Chem. 257: 3018-3025.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3018-3025
    • Bennetzen, J.L.1    Hall, B.D.2
  • 6
    • 0027386619 scopus 로고
    • Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus
    • Blamey, J. M., and M. W. W. Adams. 1993. Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcus furiosus. Biochim. Biophys. Acta 1161:19-27.
    • (1993) Biochim. Biophys. Acta , vol.1161 , pp. 19-27
    • Blamey, J.M.1    Adams, M.W.W.2
  • 7
    • 0028085225 scopus 로고
    • Characterization of an ancestral-type of pyruvate ferredoxin oxidoreductase from the hyperthermophlic bacterium, Thermotoga maritima
    • Blamey, J. M., and M. W. W. Adams. 1994. Characterization of an ancestral-type of pyruvate ferredoxin oxidoreductase from the hyperthermophlic bacterium, Thermotoga maritima. Biochemistry 33:1000-1007.
    • (1994) Biochemistry , vol.33 , pp. 1000-1007
    • Blamey, J.M.1    Adams, M.W.W.2
  • 8
    • 0025923076 scopus 로고
    • 420- and NADP-dependent alcohol dehydrogenases of Methanogenium liminatans and methanobacterium palustre, specific for secondary alcohols
    • 420- and NADP-dependent alcohol dehydrogenases of Methanogenium liminatans and Methanobacterium palustre, specific for secondary alcohols. Eur. J. Biochem. 200:43-51.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 43-51
    • Bleicher, K.1    Winter, J.2
  • 9
    • 0025236474 scopus 로고
    • Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus
    • Blumentals, I. I., M. Itoh, G. J. Olson, and R. M. Kelly. 1990. Role of polysulfides in reduction of elemental sulfur by the hyperthermophilic archaebacterium Pyrococcus furiosus. Appl. Environ. Microbiol. 56:1255-1262.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1255-1262
    • Blumentals, I.I.1    Itoh, M.2    Olson, G.J.3    Kelly, R.M.4
  • 10
    • 0031055738 scopus 로고    scopus 로고
    • Thermoanaerobacter brockii alcohol dehydrogenase: Characterization of the active site metal and its ligand amino acids
    • Bogin, O., M. Peretz, and Y. Burstein. 1997. Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids. Protein Sci. 6:450-458.
    • (1997) Protein Sci. , vol.6 , pp. 450-458
    • Bogin, O.1    Peretz, M.2    Burstein, Y.3
  • 11
    • 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
  • 12
    • 0024978145 scopus 로고
    • Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus
    • Bryant, F. O., and M. W. W. Adams. 1989. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J. Biol. Chem. 264:5070-5079.
    • (1989) J. Biol. Chem. , vol.264 , pp. 5070-5079
    • Bryant, F.O.1    Adams, M.W.W.2
  • 13
    • 0017413173 scopus 로고
    • Inhibition of methylene blue formation during determination of acid-labile sulfide of iron-sulfur protein samples containing dithionite
    • Chen, J.-S., and L. E. Mortenson. 1977. Inhibition of methylene blue formation during determination of acid-labile sulfide of iron-sulfur protein samples containing dithionite. Anal. Biochem. 79:157-165.
    • (1977) Anal. Biochem. , vol.79 , pp. 157-165
    • Chen, J.-S.1    Mortenson, L.E.2
  • 14
    • 0024723183 scopus 로고
    • The fermentation pathways of Escherichia coli
    • Clarke, D. P. 1989. The fermentation pathways of Escherichia coli. FEMS Microhiol. Rev. 63:223-234.
    • (1989) FEMS Microhiol. Rev. , vol.63 , pp. 223-234
    • Clarke, D.P.1
  • 15
    • 0023267608 scopus 로고
    • Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis
    • Conway, T., G. W. Sewell, Y. A. Osman, and L. O. Ingram. 1987. Cloning and sequencing of the alcohol dehydrogenase II gene from Zymomonas mobilis. J. Bacteriol. 169:2591-2597.
    • (1987) J. Bacteriol. , vol.169 , pp. 2591-2597
    • Conway, T.1    Sewell, G.W.2    Osman, Y.A.3    Ingram, L.O.4
  • 17
    • 0009290576 scopus 로고
    • Guide to protein purification
    • Deutscher, M. P. 1990. Guide to protein purification. Methods Enzymol. 182:588-604.
    • (1990) Methods Enzymol. , vol.182 , pp. 588-604
    • Deutscher, M.P.1
  • 18
    • 0023926199 scopus 로고
    • Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces
    • Drewke, C., and M. Ciriacy. 1988. Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces. Biochim. Biophys. Acta 950:54-60.
    • (1988) Biochim. Biophys. Acta , vol.950 , pp. 54-60
    • Drewke, C.1    Ciriacy, M.2
  • 20
    • 0022445886 scopus 로고
    • Pyrococcus furiosus sp. nov. Represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C
    • Fiala, G., and K. O. Stetter. 1986. Pyrococcus furiosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally at 100°C. Arch. Microbiol. 145:56-61.
    • (1986) Arch. Microbiol. , vol.145 , pp. 56-61
    • Fiala, G.1    Stetter, K.O.2
  • 22
    • 0024849185 scopus 로고
    • Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli
    • Goodlove, P. E., S. M. Bury, and L. Sawyer. 1989. Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene 85:209-214.
    • (1989) Gene , vol.85 , pp. 209-214
    • Goodlove, P.E.1    Bury, S.M.2    Sawyer, L.3
  • 23
    • 0031437663 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic archacon Pyrococcus furiosus
    • Gueguen, Y., W. G. B. Voorhorst, J. van der Oost, and W. M. de Vos. 1997. Molecular and biochemical characterization of an endo-β-1,3-glucanase of the hyperthermophilic archacon Pyrococcus furiosus. J. Biol. Chem. 272: 31258-31264.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31258-31264
    • Gueguen, Y.1    Voorhorst, W.G.B.2    Van Der Oost, J.3    De Vos, W.M.4
  • 24
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg, E. L., and L. Que, Jr. 1997. The 2-His-1-carboxylate facial triad: an emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur. J. Biochem. 250:625-629.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que L., Jr.2
  • 25
    • 0029149929 scopus 로고
    • Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archeon Thermococcus strain ES-1
    • Heider, J., K. Ma, and M. W. W. Adams. 1995. Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archeon Thermococcus strain ES-1. J. Bacteriol. 177:4757-4764.
    • (1995) J. Bacteriol. , vol.177 , pp. 4757-4764
    • Heider, J.1    Ma, K.2    Adams, M.W.W.3
  • 26
    • 0025972739 scopus 로고
    • Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric operon particle encoded by adhE
    • Kessler, D., I. Leibrecht, and J. Knappe. 1991. Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric operon particle encoded by adhE. FEBS Lett. 281:59-63.
    • (1991) FEBS Lett. , vol.281 , pp. 59-63
    • Kessler, D.1    Leibrecht, I.2    Knappe, J.3
  • 27
    • 0026662009 scopus 로고
    • Ultrastructure and pyruvate-quenching property of the multienzyme AdhE protein of Escherichia coli
    • Kessler, D., W. Herth, and J. Knappe. 1992. Ultrastructure and pyruvate-quenching property of the multienzyme AdhE protein of Escherichia coli. J. Biol. Chem. 267:18073-18079.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18073-18079
    • Kessler, D.1    Herth, W.2    Knappe, J.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0027405182 scopus 로고
    • Anaerobic regulation of the adhE gene, encoding the fermentative alcohol dehydrogenase of Escherichia coli
    • Leonardo, M. R., P. R. Cunningham, and D. P. Clark. 1993. Anaerobic regulation of the adhE gene, encoding the fermentative alcohol dehydrogenase of Escherichia coli. J. Bacteriol. 175:870-878.
    • (1993) J. Bacteriol. , vol.175 , pp. 870-878
    • Leonardo, M.R.1    Cunningham, P.R.2    Clark, D.P.3
  • 30
    • 0029814919 scopus 로고    scopus 로고
    • Role of NAD in regulating the adhE gene of Escherichia coli
    • Leonardo, M. R., Y. Dailly, and D. P. Clark. 1996. Role of NAD in regulating the adhE gene of Escherichia coli. J. Bacteriol. 178:6013-6018.
    • (1996) J. Bacteriol. , vol.178 , pp. 6013-6018
    • Leonardo, M.R.1    Dailly, Y.2    Clark, D.P.3
  • 31
    • 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
  • 32
    • 0001615959 scopus 로고
    • Mechanistic aspects of dihydroxybenzoate dioxygenases
    • H. Sigel and A. Sigel (ed.), Marcel Dekker, New York, N.Y.
    • Lipscomb, J. D., and A. M. Orville. 1992. Mechanistic aspects of dihydroxybenzoate dioxygenases. p. 243-298. In H. Sigel and A. Sigel (ed.), Metal ions in biological systems, vol. 28. Marcel Dekker, New York, N.Y.
    • (1992) Metal Ions in Biological Systems , vol.28 , pp. 243-298
    • Lipscomb, J.D.1    Orville, A.M.2
  • 34
    • 0028069713 scopus 로고
    • Purification and characterization of NADP-specific alcohol dehydrogenase and NADP-specific glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
    • Ma, K., F. T. Robb, and M. W. W. Adams. 1994. Purification and characterization of NADP-specific alcohol dehydrogenase and NADP-specific 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
  • 35
    • 0030932016 scopus 로고    scopus 로고
    • Pyruvate ferredoxin 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 ferredoxin oxidoreductase from the hyperthermophilic archaeon. Pyrococcus furiosus, functions as a CoA-dependent pyruvate decarboxylase. Proc. Natl. Acad. Sci. USA 94:9608-9613.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9608-9613
    • Ma, K.1    Hutchins, A.2    Sung, S.-J.S.3    Adams, M.W.W.4
  • 36
    • 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.A.1    Adams, M.W.W.2
  • 37
    • 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
  • 38
    • 0027163125 scopus 로고
    • Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
    • Ma, K., R. N. Schicho, R. M. Kelly, and M. W. W. Adams. 1993. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc. Natl. Acad. Sci. USA 90:5341-5344.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5341-5344
    • Ma, K.1    Schicho, R.N.2    Kelly, R.M.3    Adams, M.W.W.4
  • 39
    • 0027989417 scopus 로고
    • Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon. Pyrococcus furiosus: A key role for NADPH
    • Ma, K., Z. H. Zhou, and M. W. W. Adams. 1994. Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon. Pyrococcus furiosus: a key role for NADPH. FEMS Microbiol. Lett. 122:263-266.
    • (1994) FEMS Microbiol. Lett. , vol.122 , pp. 263-266
    • Ma, K.1    Zhou, Z.H.2    Adams, M.W.W.3
  • 40
    • 0012015230 scopus 로고
    • Characterization of aromatic and aliphatic 2-ketoacid oxidoreductases from hyperthermophilic archaea
    • Mai, X., and M. W. W. Adams. 1993 Characterization of aromatic and aliphatic 2-ketoacid oxidoreductases from hyperthermophilic archaea. J. Inorg. Chem. 51:459.
    • (1993) J. Inorg. Chem. , vol.51 , pp. 459
    • Mai, X.1    Adams, M.W.W.2
  • 41
    • 0028244070 scopus 로고
    • Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon. Pyrococcus furiosus: A new enzyme involved in peptide fermentation
    • Mai, X., and M. W. W. Adams. 1994. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon. Pyrococcus furiosus: a new enzyme involved in peptide fermentation. J. Biol. Chem. 269:16726-16732.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16726-16732
    • Mai, X.1    Adams, M.W.W.2
  • 42
    • 0030862385 scopus 로고    scopus 로고
    • Regulation of expression of the ethanol dehydrogenase gene (adhE) in Escherichia coli by catabolite repressor activator protein Cra
    • Mikulskis, A., A. Aristarkhov, and E. C. Lin. 1997. Regulation of expression of the ethanol dehydrogenase gene (adhE) in Escherichia coli by catabolite repressor activator protein Cra. J. Bacteriol. 179:7129-7134.
    • (1997) J. Bacteriol. , vol.179 , pp. 7129-7134
    • Mikulskis, A.1    Aristarkhov, A.2    Lin, E.C.3
  • 43
    • 0026321415 scopus 로고
    • The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase: Evidence for its participation in a unique glycolytic pathway
    • Mukund, S., and M. W. W. Adams. 1991. The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase: evidence for its participation in a unique glycolytic pathway. J. Biol. Chem 266:14208-14216.
    • (1991) J. Biol. Chem , vol.266 , pp. 14208-14216
    • Mukund, S.1    Adams, M.W.W.2
  • 44
    • 0027493772 scopus 로고
    • Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the extremely thermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism
    • Mukund, S., and M. W. W. Adams. 1993. Characterization of a novel tungsten-containing formaldehyde ferredoxin oxidoreductase from the extremely thermophilic archaeon, Thermococcus litoralis. A role for tungsten in peptide catabolism. J. Biol. Chem. 268:13592-13600.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13592-13600
    • Mukund, S.1    Adams, M.W.W.2
  • 45
    • 0344696280 scopus 로고    scopus 로고
    • National Institute of Technology and Evaluation, Tokyo, Japan
    • National Institute of Technology and Evaluation. http://www.bio.nite.go.jp/ E-home/biomenu-e2.html. National Institute of Technology and Evaluation, Tokyo, Japan.
  • 46
    • 0023039990 scopus 로고
    • The two alcohol dehydrogenases of Zymomonas mobilis - Purification by different dye ligand chromatography, molecular characterization and physiological roles
    • Neale, A. D., R. K. Scope, J. M. Kelly, and R. E. H. Wettenhall. 1986. The two alcohol dehydrogenases of Zymomonas mobilis - purification by different 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    Scope, R.K.2    Kelly, J.M.3    Wettenhall, R.E.H.4
  • 47
    • 0024327951 scopus 로고
    • Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii
    • Peretz, M., and Y. Burstein. 1989. Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii. Biochem. J. 28:6549-6555.
    • (1989) Biochem. J. , vol.28 , pp. 6549-6555
    • Peretz, M.1    Burstein, Y.2
  • 48
    • 0025883535 scopus 로고
    • Characterization of short-chain alcohol dehydrogenases and related enzymes
    • Persson, B., M. Krook, and Jörnvall. 1991. Characterization of short-chain alcohol dehydrogenases and related enzymes. Eur. J. Biochem. 200:537-543.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 537-543
    • Persson, B.1    Krook, M.2    Jörnvall3
  • 49
    • 0028241230 scopus 로고
    • Excretion of butyraldehyde, isobutyraldehyde and valeraldehyde by Streptomyces cinnamonensis
    • Pospísil, S., P. Sedmera, V. Havlícek, and V. Prikrylová. 1994. Excretion of butyraldehyde, isobutyraldehyde and valeraldehyde by Streptomyces cinnamonensis. FEMS Microbiol. Lett. 119:95-98.
    • (1994) FEMS Microbiol. Lett. , vol.119 , pp. 95-98
    • Pospísil, S.1    Sedmera, P.2    Havlícek, V.3    Prikrylová, V.4
  • 50
    • 0030061946 scopus 로고    scopus 로고
    • Activation of Sulfolobus solfataricus alcohol dehydrogenase by modification of cysteine residue 38 with iodoacetic acid
    • Raia, C. A., C. Caruso, M. Marino, N. Vespa, and M. Rossi. 1996. Activation of Sulfolobus solfataricus alcohol dehydrogenase by modification of cysteine residue 38 with iodoacetic acid. Biochemistry 35:638-647.
    • (1996) Biochemistry , vol.35 , pp. 638-647
    • Raia, C.A.1    Caruso, C.2    Marino, M.3    Vespa, N.4    Rossi, M.5
  • 51
    • 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
  • 52
    • 0023656081 scopus 로고
    • A novel archaebacterial NAD-dependent alcohol dehydrogenase: Purification and properties
    • Rella, R., C. A. Raia, M. Pensa, F. M. Pisani, A. Gambacorta, M. De Rosa, and M. Rossi. 1987. A novel archaebacterial NAD-dependent alcohol dehydrogenase: purification and properties. J. Biochem. 167:475-479.
    • (1987) J. Biochem. , vol.167 , pp. 475-479
    • Rella, R.1    Raia, C.A.2    Pensa, M.3    Pisani, F.M.4    Gambacorta, A.5    De Rosa, M.6    Rossi, M.7
  • 53
    • 0026589218 scopus 로고
    • Characterization of an extremely thermostable glutamate dehydrogenase: A key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus
    • Robb, F. T., J.-B. Park, and M. W. W. Adams. 1992. Characterization of an extremely thermostable glutamate dehydrogenase: a key enzyme in the primary metabolism of the hyperthermophilic archaebacterium, Pyrococcus furiosus. Biochim. Biophys. Acta 1120:267-272.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 267-272
    • Robb, F.T.1    Park, J.-B.2    Adams, M.W.W.3
  • 54
    • 0030875412 scopus 로고    scopus 로고
    • The phylogenetic position of the Thermococcus isolate AN1 based on 16s rRNA gene sequence analysis: A proposal that AN1 represents a new species. Thermococcus zilligii sp. nov
    • Ronimus, R. S., A.-L. Reysenbach, D. R. Musgrave, H. W. Morgan. 1997. The phylogenetic position of the Thermococcus isolate AN1 based on 16S rRNA gene sequence analysis: a proposal that AN1 represents a new species. Thermococcus zilligii sp. nov. Arch. Microbiol. 168:245-248.
    • (1997) Arch. Microbiol. , vol.168 , pp. 245-248
    • Ronimus, R.S.1    Reysenbach, A.-L.2    Musgrave, D.R.3    Morgan, H.W.4
  • 55
    • 0344696279 scopus 로고    scopus 로고
    • Unpublished results
    • Roy, R., and M. W. W. Adams. 1998. Unpublished results.
    • (1998)
    • Roy, R.1    Adams, M.W.W.2
  • 56
    • 0027329154 scopus 로고
    • Acetyl CoA synthetase (ADP-forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis
    • Schäfer, T., M. Selig, and P. Schönheit. 1993. Acetyl CoA synthetase (ADP-forming) in archaea, a novel enzyme involved in acetate formation and ATP synthesis. Arch. Microbiol. 159:72-83.
    • (1993) Arch. Microbiol. , vol.159 , pp. 72-83
    • Schäfer, T.1    Selig, M.2    Schönheit, P.3
  • 57
    • 0027175993 scopus 로고
    • Bacterial sulfur respiration
    • Schauder, R., and A. Kröger. 1993. Bacterial sulfur respiration. Arch. Microbiol. 159:491-497.
    • (1993) Arch. Microbiol. , vol.159 , pp. 491-497
    • Schauder, R.1    Kröger, A.2
  • 58
    • 0027486711 scopus 로고
    • Polysulfide as a possible substrate for sulfur-reducing bacteria
    • Schauder, R., and E. Müller. 1993. Polysulfide as a possible substrate for sulfur-reducing bacteria. Arch. Microbiol. 160:377-382.
    • (1993) Arch. Microbiol. , vol.160 , pp. 377-382
    • Schauder, R.1    Müller, E.2
  • 59
    • 0027462194 scopus 로고
    • Bioenergetics of sulfur reduction in the hyperthermophilic archaeon Pyrococcus furiosus
    • Schico, R. N., K. Ma, M. W. W. Adams, and R. M. Kelly. 1993. Bioenergetics of sulfur reduction in the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 175:1823-1830.
    • (1993) J. Bacteriol. , vol.175 , pp. 1823-1830
    • Schico, R.N.1    Ma, K.2    Adams, M.W.W.3    Kelly, R.M.4
  • 60
    • 0020555628 scopus 로고
    • An iron-activated alcohol dehydrogenase
    • Scopes, R. K. 1983. An iron-activated alcohol dehydrogenase. FEBS Lett. 156:303-306.
    • (1983) FEBS Lett. , vol.156 , pp. 303-306
    • Scopes, R.K.1
  • 61
    • 0001999440 scopus 로고
    • Diversity of extremely thermophilic archaebacteria
    • T. D. Brock (ed.), John Wiley, New York, N.Y.
    • Stetter, K. O. 1986. Diversity of extremely thermophilic archaebacteria, p. 39-74. In T. D. Brock (ed.), The thermophiles: general, molecular, and applied microbiology. John Wiley, New York, N.Y.
    • (1986) The Thermophiles: General, Molecular, and Applied Microbiology , pp. 39-74
    • Stetter, K.O.1
  • 62
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • Stetter, K. O. 1996. Hyperthermophilic procaryotes. FEMS Microbiol. Rev. 18:149-158.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 64
    • 0005614132 scopus 로고
    • Chemical reactivities of catalytic and noncatalytic zinc or cobalt atoms of horse liver alcohol dehydrogenase: Differentiation by their thermodynamic and kinetic properties
    • Sytkowski, A. J., and B. L. Vallee. 1976. Chemical reactivities of catalytic and noncatalytic zinc or cobalt atoms of horse liver alcohol dehydrogenase: differentiation by their thermodynamic and kinetic properties. Proc. Natl. Acad. Sci. USA 73:344-348.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 344-348
    • Sytkowski, A.J.1    Vallee, B.L.2
  • 65
    • 0031046388 scopus 로고    scopus 로고
    • Differential inactivation of alcohol dehydrogenase isoenzymes in Zymomonas mobilis by oxygen
    • Tamarit, J., E. Cabiscol, J. Aguilar, and J. Ros. 1997. Differential inactivation of alcohol dehydrogenase isoenzymes in Zymomonas mobilis by oxygen. J. Bacteriol. 179:1102-1104.
    • (1997) J. Bacteriol. , vol.179 , pp. 1102-1104
    • Tamarit, J.1    Cabiscol, E.2    Aguilar, J.3    Ros, J.4
  • 66
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., K. Jungermann, and K. Decker. 1977. Energy conservation in chemotrophic anaerobic bacteria. Bacteriol. Rev. 41:100-180.
    • (1977) Bacteriol. Rev. , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 67
    • 0023837957 scopus 로고
    • An iron-activated alcohol dehydrogenase: Metal dissociation constants and magnetic and spectroscopic properties
    • Tse, P., R. K. Scopes, and A. G. Wedd. 1988. An iron-activated alcohol dehydrogenase: metal dissociation constants and magnetic and spectroscopic properties. J. Am. Chem. Soc. 110:1295-1297.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1295-1297
    • Tse, P.1    Scopes, R.K.2    Wedd, A.G.3
  • 68
    • 0024638161 scopus 로고
    • The primary structure of alcohol dehydrogenase from Drosophila lebanonensis: Intensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc
    • Villarroya, A., E. Juan, B. Egestad, and H. Joenvall. 1989. The primary structure of alcohol dehydrogenase from Drosophila lebanonensis: intensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc. Eur. J. Biochem. 180:191-197.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 191-197
    • Villarroya, A.1    Juan, E.2    Egestad, B.3    Joenvall, H.4
  • 69
    • 0028876332 scopus 로고
    • Characterization of the celB gene coding for β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli
    • Voorhorst, W. G. B., R. I. L. Eggen, E. J. Luesink, and W. M. de Vos. 1995. Characterization of the celB gene coding for β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli. J. Bacteriol. 177:7105-7111.
    • (1995) J. Bacteriol. , vol.177 , pp. 7105-7111
    • Voorhorst, W.G.B.1    Eggen, R.I.L.2    Luesink, E.J.3    De Vos, W.M.4
  • 70
    • 0344264618 scopus 로고    scopus 로고
    • Unpublished data
    • Weiss, R. B. Unpublished data.
    • Weiss, R.B.1
  • 71
    • 0025300402 scopus 로고
    • Towards a natural system of organisms: Proposal for the domains of Archaea, Bacteria and Eucarya
    • Woese, C. R., O. Kandler, and M. L. Wheelis. 1990. Towards a natural system of organisms: proposal for the domains of Archaea, Bacteria and Eucarya. Proc. Natl. Acad. Sci. USA 87:4576-4579.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4576-4579
    • Woese, C.R.1    Kandler, O.2    Wheelis, M.L.3
  • 72
    • 0027293730 scopus 로고
    • Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: A new extradiol catecholic dioxygenase
    • Wolgel, S. A., J. E. Dege, P. E. Perkins-Olson, C. H. Juarez-Garcia, R. L. Crawford, E. Münck, and J. D. Lipscomb. 1993. Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase. J. Bacteriol. 175:4414-4426.
    • (1993) J. Bacteriol. , vol.175 , pp. 4414-4426
    • Wolgel, S.A.1    Dege, J.E.2    Perkins-Olson, P.E.3    Juarez-Garcia, C.H.4    Crawford, R.L.5    Münck, E.6    Lipscomb, J.D.7


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