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Volumn 78, Issue 6, 2012, Pages 1724-1732

Rhodococcus sp. strain CR-53 lipr, the first member of a new bacterial lipase family (Family X) displaying an unusual Y-type oxyanion hole, similar to the Candida antarctica lipase clan

Author keywords

[No Author keywords available]

Indexed keywords

ACYL GROUP; AMINO ACID SEQUENCE; AMINO ACID SEQUENCE MOTIFS; BIOINFORMATICS TOOLS; BURKHOLDERIA; CANDIDA ANTARCTICA; CHEMICAL AGENT; INFORMATION CONCERNING; INTERFACIAL ACTIVATION; LONG TERM STABILITY; MESOPHILIC; OXYANION HOLE; REACTION MIXTURE; RHODOCOCCUS; RHODOCOCCUS SP; SYNTHETIC ORGANIC CHEMISTRY;

EID: 84857887080     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.06332-11     Document Type: Article
Times cited : (33)

References (46)
  • 1
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, 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
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny JL, Jaeger K-E. 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
    • 77649274388 scopus 로고    scopus 로고
    • Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA
    • Bofill C, et al. 2010. Differential behaviour of Pseudomonas sp. 42A2 LipC, a lipase showing greater versatility than its counterpart LipA. Biochimie 92:307-316.
    • (2010) Biochimie , vol.92 , pp. 307-316
    • Bofill, C.1
  • 5
    • 0003996567 scopus 로고
    • Chapman & Hall, London, United Kingdom
    • Britton HTS. 1952. Hydrogen ions. Chapman & Hall, London, United Kingdom.
    • (1952) Hydrogen ions
    • Britton, H.T.S.1
  • 6
    • 23144444979 scopus 로고    scopus 로고
    • Protein structure prediction servers at University College London
    • Bryson K, et al. 2005. Protein structure prediction servers at University College London. Nucleic Acids Res. 33:W36-W38.
    • (2005) Nucleic Acids Res , vol.33
    • Bryson, K.1
  • 8
    • 0032869128 scopus 로고    scopus 로고
    • Direct fluorescence-based lipase activity assay
    • 700
    • Diaz P, Prim N, Pastor FIJ. 1999. Direct fluorescence-based lipase activity assay. Biotechniques 27:696-698, 700.
    • (1999) Biotechniques , vol.27 , pp. 696-698
    • Diaz, P.1    Prim, N.2    Pastor, F.I.J.3
  • 9
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP, and related tools
    • Emanuelsson O, Brunak S, von Heijne G, Nielsen H. 2007. Locating proteins in the cell using TargetP, SignalP, and related tools. Nat. Protoc. 2:953-971.
    • (2007) Nat. Protoc. , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 10
    • 38049012808 scopus 로고    scopus 로고
    • X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation
    • Ericsson DJ, et al. 2008. X-ray structure of Candida antarctica lipase A shows a novel lid structure and a likely mode of interfacial activation. J. Mol. Biol. 376:109 -119.
    • (2008) J. Mol. Biol. , vol.376 , pp. 109-119
    • Ericsson, D.J.1
  • 11
  • 12
    • 33747063093 scopus 로고    scopus 로고
    • Propionibacterium acnes GehA lipase, an enzyme involved in acne development, can be successfully inhibited by defined natural substances
    • Falcocchio S, Ruiz C, Pastor FIJ, Saso L, Diaz P. 2006. Propionibacterium acnes GehA lipase, an enzyme involved in acne development, can be successfully inhibited by defined natural substances. J. Mol. Catalysis B Enzymatic 40:132-137.
    • (2006) J. Mol. Catalysis B Enzymatic , vol.40 , pp. 132-137
    • Falcocchio, S.1    Ruiz, C.2    Pastor, F.I.J.3    Saso, L.4    Diaz, P.5
  • 13
    • 33751255103 scopus 로고    scopus 로고
    • DWARF-a data warehouse system for analyzing protein families
    • Fischer M, Thai QK, Grieb M, Pleiss J. 2006. DWARF-a data warehouse system for analyzing protein families. BMC Bioinformatics 7:495.
    • (2006) BMC Bioinformatics , vol.7 , pp. 495
    • Fischer, M.1    Thai, Q.K.2    Grieb, M.3    Pleiss, J.4
  • 14
    • 0033653715 scopus 로고    scopus 로고
    • What distinguishes an esterase from a lipase: a novel structural approach
    • Fojan P, Jonson PH, Petersen MTN, Petersen SB. 2000. What distinguishes an esterase from a lipase: a novel structural approach. Biochimie 82:1033-1041.
    • (2000) Biochimie , vol.82 , pp. 1033-1041
    • Fojan, P.1    Jonson, P.H.2    Petersen, M.T.N.3    Petersen, S.B.4
  • 15
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • Frickey T, Lupas A. 2004. CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics 20:3702- 3704.
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 16
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: an overview of production, purification and biochemical properties
    • Gupta R, Gupta N, Rathi P. 2004. Bacterial lipases: an overview of production, purification and biochemical properties. Appl. Microbiol. Biotechnol. 64:763-781.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 17
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T. 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp. Ser. 41:95-98.
    • (1999) Nucleic Acids Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.1
  • 19
    • 0038236305 scopus 로고    scopus 로고
    • A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases
    • Henke E, Bornscheuer UT, Schmid RD, Pleiss J. 2003. A molecular mechanism of enantiorecognition of tertiary alcohols by carboxylesterases. Chem. Eur. J. Chem. Biol. 4:485- 493.
    • (2003) Chem. Eur. J. Chem. Biol. , vol.4 , pp. 485-493
    • Henke, E.1    Bornscheuer, U.T.2    Schmid, R.D.3    Pleiss, J.4
  • 21
    • 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
  • 22
    • 45949107473 scopus 로고    scopus 로고
    • Recent developments in the MAFFT multiple sequence alignment program
    • Katoh K, Toh H. 2008. Recent developments in the MAFFT multiple sequence alignment program. Brief. Bioinformatics 9:286 -298.
    • (2008) Brief. Bioinformatics 9 , pp. 286-298
    • Katoh, K.1    Toh, H.2
  • 23
    • 0642367795 scopus 로고
    • Asymmetric transformations catalyzed by enzymes in organic-solvents
    • Klibanov AM. 1990. Asymmetric transformations catalyzed by enzymes in organic-solvents. Accounts Chem. Res. 23:114 -120.
    • (1990) Accounts Chem. Res. , vol.23 , pp. 114-120
    • Klibanov, A.M.1
  • 24
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker G, Jaeger KE. 1987. Specific and sensitive plate assay for bacterial lipases. Appl. Environ. Microbiol. 53:211-213.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.E.2
  • 25
    • 20444371027 scopus 로고    scopus 로고
    • Biodegradation and Rhodococcus-masters of catabolic versatility
    • Larkin MJ, Kulakov LA, Allen CC. 2005. Biodegradation and Rhodococcus- masters of catabolic versatility. Curr. Opin. Biotechnol. 16:282-290.
    • (2005) Curr. Opin. Biotechnol. , vol.16 , pp. 282-290
    • Larkin, M.J.1    Kulakov, L.A.2    Allen, C.C.3
  • 26
    • 33750971458 scopus 로고    scopus 로고
    • Isolation and characterization of a novel lipase from a metagenomic library of tidal flat sediments: evidence for a new family of bacterial lipases
    • Lee M-H, Lee C-H, Oh T-K, Song JK, Yoon J-H. 2006. Isolation and characterization of a novel lipase from a metagenomic library of tidal flat sediments: evidence for a new family of bacterial lipases. Appl. Environ. Microbiol. 72:7406 -7409.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 7406-7409
    • Lee, M.-H.1    Lee, C.-H.2    Oh, T.-K.3    Song, J.K.4    Yoon, J.-H.5
  • 27
    • 78149409119 scopus 로고    scopus 로고
    • A new esterase EstD2 isolated from plant rhizosphere soil metagenome
    • Lee MH, et al. 2010. A new esterase EstD2 isolated from plant rhizosphere soil metagenome. Appl. Microbiol. Biotechnol. 88:1125-1134.
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , pp. 1125-1134
    • Lee, M.H.1
  • 28
    • 35348843459 scopus 로고    scopus 로고
    • A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp. GMD509
    • Park SY, et al. 2007. A new esterase showing similarity to putative dienelactone hydrolase from a strict marine bacterium, Vibrio sp. GMD509. Appl. Microbiol. Biotechnol. 77:107-115.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 107-115
    • Park, S.Y.1
  • 29
    • 0034078335 scopus 로고    scopus 로고
    • estA, a gene coding for a cell-bound esterase from Paenibacillus sp. BP-23, is a new member of the bacterial subclass of type B carboxylesterases
    • Prim N, Blanco A, Martinez J, Pastor FIJ, Diaz P. 2000. estA, a gene coding for a cell-bound esterase from Paenibacillus sp. BP-23, is a new member of the bacterial subclass of type B carboxylesterases. Res. Microbiol. 151:303-312.
    • (2000) Res. Microbiol. , vol.151 , pp. 303-312
    • Prim, N.1    Blanco, A.2    Martinez, J.3    Pastor, F.I.J.4    Diaz, P.5
  • 30
    • 33746479149 scopus 로고    scopus 로고
    • Esterase EstA6 from Pseudomonas sp CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes
    • Prim N, Bofill C, Pastor FIJ, Diaz P. 2006. Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes. Biochimie 88:859-867.
    • (2006) Biochimie , vol.88 , pp. 859-867
    • Prim, N.1    Bofill, C.2    Pastor, F.I.J.3    Diaz, P.4
  • 31
    • 0035098789 scopus 로고    scopus 로고
    • Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7
    • Prim N, Pastor FIJ, Diaz P. 2001. Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7. Curr. Microbiol. 42:237-240.
    • (2001) Curr. Microbiol. , vol.42 , pp. 237-240
    • Prim, N.1    Pastor, F.I.J.2    Diaz, P.3
  • 32
  • 33
    • 0030954910 scopus 로고    scopus 로고
    • Molecular analysis of the Rhodococcus sp. strain H1 her gene and characterization of its product, a heroin esterase, expressed in Escherichia coli
    • Rathbone DA, Holt PJ, Lowe CR, Bruce NC. 1997. Molecular analysis of the Rhodococcus sp. strain H1 her gene and characterization of its product, a heroin esterase, expressed in Escherichia coli. Appl. Environ. Microbiol. 63:2062-2066.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 2062-2066
    • Rathbone, D.A.1    Holt, P.J.2    Lowe, C.R.3    Bruce, N.C.4
  • 34
    • 84857870195 scopus 로고    scopus 로고
    • Directed evolution as a means to create enantioselective enzymes
    • ORGN
    • Reetz MT. 2002. Directed evolution as a means to create enantioselective enzymes. Abstr. Papers Am. Chem. Soc. 224:ORGN 302.
    • (2002) Abstr. Papers Am. Chem. Soc. , vol.224 , pp. 302
    • Reetz, M.T.1
  • 35
    • 0033646651 scopus 로고    scopus 로고
    • Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion
    • Rosenau F, Jaeger KE. 2000. Bacterial lipases from Pseudomonas: regulation of gene expression and mechanisms of secretion. Biochimie 82: 1023-1032.
    • (2000) Biochimie , vol.82 , pp. 1023-1032
    • Rosenau, F.1    Jaeger, K.E.2
  • 36
    • 0037126654 scopus 로고    scopus 로고
    • Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I 4 bacterial lipase
    • Ruiz C, Blanco A, Pastor FIJ, Diaz P. 2002. Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase. FEMS Microbiol. Lett. 217:263-267.
    • (2002) FEMS Microbiol. Lett. , vol.217 , pp. 263-267
    • Ruiz, C.1    Blanco, A.2    Pastor, F.I.J.3    Diaz, P.4
  • 37
    • 34247585473 scopus 로고    scopus 로고
    • Helicobacter pylori EstV: identification, cloning, and characterization of the first lipase isolated from an epsilon-proteobacterium
    • Ruiz C, Falcocchio S, Pastor FIJ, Saso L, Diaz P. 2007. Helicobacter pylori EstV: identification, cloning, and characterization of the first lipase isolated from an epsilon-proteobacterium. Appl. Environ. Microbiol. 73: 2423-2431.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 2423-2431
    • Ruiz, C.1    Falcocchio, S.2    Pastor, F.I.J.3    Saso, L.4    Diaz, P.5
  • 38
    • 2942558920 scopus 로고    scopus 로고
    • Activation and inhibition of Candida rugosa and Bacillus-related lipases by saturated fatty acids, evaluated by a new colorimetric microassay
    • Ruiz C, et al. 2004. Activation and inhibition of Candida rugosa and Bacillus-related lipases by saturated fatty acids, evaluated by a new colorimetric microassay. Biochim. Biophys. Acta 1672:184 -191.
    • (2004) Biochim. Biophys. Acta , vol.1672 , pp. 184-191
    • Ruiz, C.1
  • 39
    • 0141762453 scopus 로고    scopus 로고
    • Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species
    • Ruiz C, Pastor FIJ, Diaz P. 2003. Isolation and characterization of Bacillus sp. BP-6 LipA, a ubiquitous lipase among mesophilic Bacillus species. Lett. Appl. Microbiol. 37:354 -359.
    • (2003) Lett. Appl. Microbiol. , vol.37 , pp. 354-359
    • Ruiz, C.1    Pastor, F.I.J.2    Diaz, P.3
  • 40
    • 14644408029 scopus 로고    scopus 로고
    • Isolation of lipid- and polysaccharidedegrading micro-organisms from subtropical forest soil, and analysis of lipolytic strain Bacillus sp. CR-179
    • Ruiz C, Pastor FIJ, Diaz P. 2005. Isolation of lipid- and polysaccharidedegrading micro-organisms from subtropical forest soil, and analysis of lipolytic strain Bacillus sp. CR-179. Lett. Appl. Microbiol. 40:218 -227.
    • (2005) Lett. Appl. Microbiol. , vol.40 , pp. 218-227
    • Ruiz, C.1    Pastor, F.I.J.2    Diaz, P.3
  • 43
    • 33644854755 scopus 로고    scopus 로고
    • Sequence analysis of three plasmids harboured in Rhodococcus erythropolis strain PR4
    • Sekine M, et al. 2006. Sequence analysis of three plasmids harboured in Rhodococcus erythropolis strain PR4. Environ. Microbiol. 8:334 -346.
    • (2006) Environ. Microbiol. , vol.8 , pp. 334-346
    • Sekine, M.1
  • 44
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K, Dudley J, Nei M, Kumar S. 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
  • 45
  • 46
    • 77950382453 scopus 로고    scopus 로고
    • Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A
    • Widmann M, Juhl PB, Pleiss J. 2010. Structural classification by the Lipase Engineering Database: a case study of Candida antarctica lipase A. BMC Genomics 11:123.
    • (2010) BMC Genomics , vol.11 , pp. 123
    • Widmann, M.1    Juhl, P.B.2    Pleiss, J.3


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