메뉴 건너뛰기




Volumn 13, Issue 2, 2009, Pages 299-311

Molecular characterization of the recombinant iron-containing alcohol dehydrogenase from the hyperthermophilic Archaeon, Thermococcus strain ES1

Author keywords

Archaea; Heterologous expression; Hyperthermophile; Iron containing alcohol dehydrogenase; Thermococcus

Indexed keywords

ALCOHOL DEHYDROGENASE; IRON; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT PROTEIN;

EID: 61449240010     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-008-0217-z     Document Type: Article
Times cited : (19)

References (43)
  • 2
    • 0033568692 scopus 로고    scopus 로고
    • Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis
    • E Antoine JL Rolland JP Raffin 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
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • MM Bradford 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
  • 5
    • 0030046289 scopus 로고    scopus 로고
    • Cloning and overexpression in Escherichia coli of the genes encoding NAD-dependent alcohol dehydrogenase from two Sulfolobus species
    • R Cannio G Fiorentino P Carpinelli M Rossi 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
  • 6
    • 0024342310 scopus 로고
    • Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae
    • T Conway LO Ingram 1989 Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae J Bacteriol 171 3754 3759
    • (1989) J Bacteriol , vol.171 , pp. 3754-3759
    • Conway, T.1    Ingram, L.O.2
  • 7
    • 61449168205 scopus 로고    scopus 로고
    • Delano Scientific Palo Alto
    • Delano WL (2002) The PyMOL molecular graphics system. Delano Scientific, Palo Alto
    • (2002)
    • Delano, W.L.1
  • 9
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • N Guex MC Peitsch 1997 SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling Electrophoresis 18 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 10
    • 1842451878 scopus 로고    scopus 로고
    • Properties of an alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix K1
    • H Hirakawa N Kamiya Y Kawarabayashi 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
  • 11
    • 0033768654 scopus 로고    scopus 로고
    • Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acid
    • CA Holland-Staley K Lee DP Clark PR Cunningham 2000 Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acid J Bacteriol 182 6049 6054
    • (2000) J Bacteriol , vol.182 , pp. 6049-6054
    • Holland-Staley, C.A.1    Lee, K.2    Clark, D.P.3    Cunningham, P.R.4
  • 12
    • 0033485581 scopus 로고    scopus 로고
    • Large-scale applications of NAD(P)-dependent oxidoreductases: Recent developments
    • W Hummel 1999 Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments Trends Biotechnol 17 487 492
    • (1999) Trends Biotechnol , vol.17 , pp. 487-492
    • Hummel, W.1
  • 13
    • 0028036503 scopus 로고
    • Characterization of an extremely thermophilic sulphur-metabolizing archaebacterium belonging to the Thermococcales
    • KU Klages HW Morgan 1994 Characterization of an extremely thermophilic sulphur-metabolizing archaebacterium belonging to the Thermococcales Arch Microbiol 162 261 266
    • (1994) Arch Microbiol , vol.162 , pp. 261-266
    • Klages, K.U.1    Morgan, H.W.2
  • 14
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of annotated three-dimensional protein structure homology models
    • J Kopp 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
  • 15
    • 33745711929 scopus 로고    scopus 로고
    • Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli
    • J Kube C Brokamp R Machielsen J van der Oost H Märkl 2006 Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli Extremophiles 10 221 227
    • (2006) Extremophiles , vol.10 , pp. 221-227
    • Kube, J.1    Brokamp, C.2    MacHielsen, R.3    Van Der Oost, J.4    Märkl, H.5
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • UK Laemmli 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
  • 17
    • 0020794694 scopus 로고
    • Rapid and sensitive colorimetric method for visualization of biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: Bioblots
    • JJ Leary DJ Brigati DC Ward 1983 Rapid and sensitive colorimetric method for visualization of biotin-labeled DNA probes hybridized to DNA or RNA immobilized on nitrocellulose: bioblots Proc Natl Acad Sci USA 80 4045 4049
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 4045-4049
    • Leary, J.J.1    Brigati, D.J.2    Ward, D.C.3
  • 18
    • 0030878620 scopus 로고    scopus 로고
    • Purification and sequence analysis of a novel NADP(H)-dependent type III alcohol dehydrogenase from Thermococcus strain AN1
    • D Li KJ 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
  • 20
    • 0032988361 scopus 로고    scopus 로고
    • An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus
    • K Ma MWW Adams 1999 An unusual oxygen-sensitive, iron- and zinc-containing alcohol dehydrogenase from the hyperthermophilic archaeon, Pyrococcus furiosus J Bacteriol 181 1163 1170
    • (1999) J Bacteriol , vol.181 , pp. 1163-1170
    • Ma, K.1    Adams, M.W.W.2
  • 21
    • 0035078332 scopus 로고    scopus 로고
    • Alcohol dehydrogenases from Thermococcus litoralis and Thermococcus strain ES-1
    • K Ma MWW Adams 2001 Alcohol dehydrogenases from Thermococcus litoralis and Thermococcus strain ES-1 Meth Enzymol 331 195 201
    • (2001) Meth Enzymol , vol.331 , pp. 195-201
    • Ma, K.1    Adams, M.W.W.2
  • 22
    • 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
    • K Ma H Loessner J Heider MK Johnson MWW 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
  • 23
    • 0028069713 scopus 로고
    • Purification and characterization of NADP-specific alcohol dehydrogenase and glutamate dehydrogenase from the hyperthermophilic archaeon Thermococcus litoralis
    • K Ma FT Robb MWW Adams 1994 Purification and characterization of NADP-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
  • 24
    • 33644855821 scopus 로고    scopus 로고
    • Production and characterization of a thermostable alcohol dehydrogenase that belongs to the aldo-keto reductase superfamily
    • R Machielsen AR Uria SWM Kengen 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
  • 25
    • 21844439989 scopus 로고    scopus 로고
    • Crystal structure of an iron-dependent group III dehydrogenase that interconverts l-lactaldehyde and l-1,2-propanediol in Escherichia coli
    • C Montella L Bellsolell R Pérez-Luque J Badía L Baldoma M Coll J Aguilar 2005 Crystal structure of an iron-dependent group III dehydrogenase that interconverts l-lactaldehyde and l-1,2-propanediol in Escherichia coli J Bacteriol 187 4957 4966
    • (2005) J Bacteriol , vol.187 , pp. 4957-4966
    • Montella, C.1    Bellsolell, L.2    Pérez-Luque, R.3    Badía, J.4    Baldoma, L.5    Coll, M.6    Aguilar, J.7
  • 26
    • 0023039990 scopus 로고
    • The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation and physiological roles
    • AD Neale RK Scopes JM Kelly RE Wettenhall 1986 The two alcohol dehydrogenases of Zymomonas mobilis. Purification by differential dye ligand chromatography, molecular characterisation 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.4
  • 27
    • 0025101757 scopus 로고
    • Thermococcus litoralis sp. nov.: A new species of extremely thermophilic marine archaebacteria
    • A Neuner HW Jannasch S Belkin KO Stetter 1989 Thermococcus litoralis sp. nov.: a new species of extremely thermophilic marine archaebacteria Arch Microbiol 153 205 207
    • (1989) Arch Microbiol , vol.153 , pp. 205-207
    • Neuner, A.1    Jannasch, H.W.2    Belkin, S.3    Stetter, K.O.4
  • 28
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • MC Peitsch 1995 Protein modeling by E-mail Bio Technol 13 658 660
    • (1995) Bio Technol , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 29
    • 0024828369 scopus 로고
    • Characterization of an extremely thermophilic archaebacterium isolated from a black smoker polychaete (Paralvinella, sp.) at the Juan de Fuca Ridge
    • RJ Pledger J Baross 1989 Characterization of an extremely thermophilic archaebacterium isolated from a black smoker polychaete (Paralvinella, sp.) at the Juan de Fuca Ridge Syst Appl Microbiol 12 249 256
    • (1989) Syst Appl Microbiol , vol.12 , pp. 249-256
    • Pledger, R.J.1    Baross, J.2
  • 30
    • 0028212644 scopus 로고
    • Molecular characterization of microbial alcohol dehydrogenases
    • MF Reid CA 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
  • 31
    • 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
    • RS Ronimus AL Reysenbach DR Musgrave HW 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
  • 32
    • 61449086662 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • Sambrook J, Russell DW (2001) Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 34
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T Schwede J Kopp N Guex MC 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
  • 35
    • 0001196882 scopus 로고
    • Hyperthermophiles-physiology and enzymes
    • KO Stetter 1988 Hyperthermophiles-physiology and enzymes J Chem Technol Biotechnol 42 315 317
    • (1988) J Chem Technol Biotechnol , vol.42 , pp. 315-317
    • Stetter, K.O.1
  • 36
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • K Tamura J Dudley M Nei S Kumar 2007 MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0 Mol Biol Evol 24 1596 1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • JD Thompson DG Higgins TJ 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
  • 40
    • 0026563908 scopus 로고
    • Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes
    • KA Walter GN Bennett ET Papoutsakis 1992 Molecular characterization of two Clostridium acetobutylicum ATCC 824 butanol dehydrogenase isozyme genes J Bacteriol 174 7149 7158
    • (1992) J Bacteriol , vol.174 , pp. 7149-7158
    • Walter, K.A.1    Bennett, G.N.2    Papoutsakis, E.T.3
  • 42
    • 34249041759 scopus 로고    scopus 로고
    • Purification and characterization of an iron-containing alcohol dehydrogenase in extremely thermophilic bacterium Thermotoga hypogea
    • X Ying Y Wang HR Badiei V Karanassios K Ma 2007 Purification and characterization of an iron-containing alcohol dehydrogenase in extremely thermophilic bacterium Thermotoga hypogea Arch Microbiol 187 499 510
    • (2007) Arch Microbiol , vol.187 , pp. 499-510
    • Ying, X.1    Wang, Y.2    Badiei, H.R.3    Karanassios, V.4    Ma, K.5
  • 43
    • 1342288664 scopus 로고    scopus 로고
    • Cloning and sequence analysis of the dhaT gene of the 1,3-propanediol regulon from Klebsiella pneumoniae
    • Y Zheng Y Cao B Fang 2004 Cloning and sequence analysis of the dhaT gene of the 1,3-propanediol regulon from Klebsiella pneumoniae Biotechnol Lett 26 251 255
    • (2004) Biotechnol Lett , vol.26 , pp. 251-255
    • Zheng, Y.1    Cao, Y.2    Fang, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.