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Volumn 74, Issue 3, 2007, Pages 585-591

Characterization of a thermostable carboxylesterase from the hyperthermophilic bacterium Thermotoga maritima

Author keywords

Alpha beta Hydrolase; Carboxylesterase; Esterase; Hyperthermophilic enzyme; Lipase; Lipolytic enzyme

Indexed keywords

CARBOXYLATION; CATALYSIS; ENZYMES; ESTERS; FLUORIDE MINERALS; GENES; GENETIC ENGINEERING; SUBSTRATES;

EID: 33847113881     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0687-9     Document Type: Article
Times cited : (41)

References (25)
  • 1
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • Arpigny JL, Jaeger KE (1999) Bacterial lipolytic enzymes: classification and properties. Biochem J 343:177-183
    • (1999) Biochem J , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 3
    • 0025734772 scopus 로고
    • Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken SM, Rozeboom HJ, Kalk KH, Dijkstra BW (1991) Crystal structure of haloalkane dehalogenase: an enzyme to detoxify halogenated alkanes. EMBO J 10:1297-1302
    • (1991) EMBO J , vol.10 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 5
    • 0027182430 scopus 로고
    • Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumae
    • Frenken LG, de Groot A, Tommassen J, Verrips CT (1993b) Role of the lipB gene product in the folding of the secreted lipase of Pseudomonas glumae. Mol Microbiol 9:591-599
    • (1993) Mol Microbiol , vol.9 , pp. 591-599
    • Frenken, L.G.1    de Groot, A.2    Tommassen, J.3    Verrips, C.T.4
  • 6
    • 17844366884 scopus 로고    scopus 로고
    • A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products
    • Fushinobu S, Jun SY, Hidaka M, Nojiri H, Yamane H, Shoun H, Omori T, Wakagi T (2005) A series of crystal structures of a meta-cleavage product hydrolase from Pseudomonas fluorescens IP01 (CumD) complexed with various cleavage products. Biosci Biotechnol Biochem 69:491-498
    • (2005) Biosci Biotechnol Biochem , vol.69 , pp. 491-498
    • Fushinobu, S.1    Jun, S.Y.2    Hidaka, M.3    Nojiri, H.4    Yamane, H.5    Shoun, H.6    Omori, T.7    Wakagi, T.8
  • 7
    • 0036324633 scopus 로고    scopus 로고
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
    • Hotta Y, Ezaki S, Atomi H, Imanaka T (2002) Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon. Appl Environ Microbiol 68:3925-3931
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3925-3931
    • Hotta, Y.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 8
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • Jaeger KE, Reetz MT (1998) Microbial lipases form versatile tools for biotechnology. Trends Biotechnol 16:396-403
    • (1998) Trends Biotechnol , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 9
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 53:315-351
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0030596528 scopus 로고    scopus 로고
    • Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution
    • Lang D, Hofmann B, Haalck L, Hecht HJ, Spener F, Schmid RD, Schomburg D (1996) Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 angstroms resolution. J Mol Biol 259:704-717
    • (1996) J Mol Biol , vol.259 , pp. 704-717
    • Lang, D.1    Hofmann, B.2    Haalck, L.3    Hecht, H.J.4    Spener, F.5    Schmid, R.D.6    Schomburg, D.7
  • 12
    • 0025234374 scopus 로고
    • Structure of wheat serine carboxypeptidase II at 3.5-Å resolution. A new class of serine proteinase
    • Liao DI, Remington SJ (1990) Structure of wheat serine carboxypeptidase II at 3.5-Å resolution. A new class of serine proteinase. J Biol Chem 265:6528-6531
    • (1990) J Biol Chem , vol.265 , pp. 6528-6531
    • Liao, D.I.1    Remington, S.J.2
  • 13
    • 0033958727 scopus 로고    scopus 로고
    • Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus
    • Manco G, Giosue E, D'Auria S, Herman P, Carrea G, Rossi M (2000) Cloning, overexpression, and properties of a new thermophilic and thermostable esterase with sequence similarity to hormone-sensitive lipase subfamily from the archaeon Archaeoglobus fulgidus. Arch Biochem Biophys 373:182-192
    • (2000) Arch Biochem Biophys , vol.373 , pp. 182-192
    • Manco, G.1    Giosue, E.2    D'Auria, S.3    Herman, P.4    Carrea, G.5    Rossi, M.6
  • 14
    • 9644275365 scopus 로고    scopus 로고
    • Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family
    • Mandrich L, Merone L, Pezzullo M, Cipolla L, Nicotra F, Rossi M, Manco G (2005) Role of the N terminus in enzyme activity, stability and specificity in thermophilic esterases belonging to the HSL family. J Mol Biol 345:501-512
    • (2005) J Mol Biol , vol.345 , pp. 501-512
    • Mandrich, L.1    Merone, L.2    Pezzullo, M.3    Cipolla, L.4    Nicotra, F.5    Rossi, M.6    Manco, G.7
  • 15
    • 0037160540 scopus 로고    scopus 로고
    • A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: Cloning of the gene, characterization of the protein
    • Morana A, Di Prizito N, Aurilia V, Rossi M, Cannio R (2002) A carboxylesterase from the hyperthermophilic archaeon Sulfolobus solfataricus: cloning of the gene, characterization of the protein. Gene 283:107-115
    • (2002) Gene , vol.283 , pp. 107-115
    • Morana, A.1    Di Prizito, N.2    Aurilia, V.3    Rossi, M.4    Cannio, R.5
  • 16
    • 0034613390 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases
    • Nardini M, Lang DA, Liebeton K, Jaeger KE, Dijkstra BW (2000) Crystal structure of Pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases. J Biol Chem 275:31219-31225
    • (2000) J Biol Chem , vol.275 , pp. 31219-31225
    • Nardini, M.1    Lang, D.A.2    Liebeton, K.3    Jaeger, K.E.4    Dijkstra, B.W.5
  • 17
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate
    • Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG (1993) The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett 331:123-128
    • (1993) FEBS Lett , vol.331 , pp. 123-128
    • Noble, M.E.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.5
  • 19
    • 26444540723 scopus 로고    scopus 로고
    • Stereoselective lipases from Burkholderia sp., cloning and their application to preparation of methyl (R)-N-(2,6- dimethylphenyl)alaninate, a key intermediate for (R)-Metalaxyl
    • Park OJ, Lee SH (2005) Stereoselective lipases from Burkholderia sp., cloning and their application to preparation of methyl (R)-N-(2,6- dimethylphenyl)alaninate, a key intermediate for (R)-Metalaxyl. J Biotechnol 120:174-182
    • (2005) J Biotechnol , vol.120 , pp. 174-182
    • Park, O.J.1    Lee, S.H.2
  • 20
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • Pathak D, Ollis D (1990) Refined structure of dienelactone hydrolase at 1.8 Å. J Mol Biol 214:497-525
    • (1990) J Mol Biol , vol.214 , pp. 497-525
    • Pathak, D.1    Ollis, D.2
  • 21
  • 24
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I (1991) Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253:872-879
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 25
    • 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 JD, Higgins DG, Gibson TJ (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.