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Volumn 45, Issue 4, 2010, Pages 475-480

Cloning, screening and characterization of ester hydrolases with enantioselectivity in typical bacteria

Author keywords

Enantioselectivity; Ester hydrolase; Esterification; Hydrolysis; Resolution

Indexed keywords

2-OCTANOL; CANDIDA RUGOSA LIPASE; CARBOXYLESTERASES; CATALYTIC ACTIVITY; COMMERCIAL ENZYMES; ESTER HYDROLASE; ESTERASE ACTIVITIES; GENOMIC INFORMATION; HIGH ACTIVITY; HYDROLASE FAMILY; HYDROLASES; PH VALUE; PHYLOGENETIC ANALYSIS; PSEUDOMONAS PUTIDA; RHODOBACTER SPHAEROIDES; SUBSTRATE SPECIFICITY;

EID: 77649188313     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.11.004     Document Type: Article
Times cited : (9)

References (27)
  • 2
  • 3
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny J.L., and Jaeger K.E. Bacterial lipolytic enzymes: classification and properties. Biochem J 343 (1999) 177-183
    • (1999) Biochem J , vol.343 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 4
    • 33748525883 scopus 로고    scopus 로고
    • Enzyme promiscuity: evolutionary and mechanistic aspects
    • Khersonsky O., Roodveldt C., and Tawfik D.S. Enzyme promiscuity: evolutionary and mechanistic aspects. Curr Opin Chem Biol 10 (2006) 498-508
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 498-508
    • Khersonsky, O.1    Roodveldt, C.2    Tawfik, D.S.3
  • 5
    • 38149122142 scopus 로고    scopus 로고
    • Catalytic promiscuity in the alpha/beta-hydrolase superfamily: hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C bond hydrolase family
    • Chen L., Hassler M., and Bugg T.D.H. Catalytic promiscuity in the alpha/beta-hydrolase superfamily: hydroxamic acid formation, C-C bond formation, ester and thioester hydrolysis in the C-C bond hydrolase family. ChemBioChem 9 (2007) 71-76
    • (2007) ChemBioChem , vol.9 , pp. 71-76
    • Chen, L.1    Hassler, M.2    Bugg, T.D.H.3
  • 6
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: the family keeps growing
    • Nardini M., and Dijkstra B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 9 (1999) 732-737
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 7
    • 0032731656 scopus 로고    scopus 로고
    • Biocatalysis for industrial production of fine chemicals
    • Schulze B., and Wubbolts M.G. Biocatalysis for industrial production of fine chemicals. Curr Opin Biotechnol 10 (1999) 609-615
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 609-615
    • Schulze, B.1    Wubbolts, M.G.2
  • 8
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools in biotechnology
    • Jaeger K.E., and Reetz M.T. Microbial lipases form versatile tools in biotechnology. Trends Biotechnol 16 (1998) 396-403
    • (1998) Trends Biotechnol , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 9
    • 29744452622 scopus 로고    scopus 로고
    • Kinetic resolution of ibuprofen in ionic liquid by Candida rugosa lipase
    • Yu H.W., and Ching C.B. Kinetic resolution of ibuprofen in ionic liquid by Candida rugosa lipase. Chirality 17 (2005) 16-21
    • (2005) Chirality , vol.17 , pp. 16-21
    • Yu, H.W.1    Ching, C.B.2
  • 10
    • 0001215393 scopus 로고    scopus 로고
    • Origin of the enantioselectivity of lipases explained by a stereo-sensing mechanism operative at the transition state
    • Ema T., Kobayashi J., Maeno S., Sakai T., and Utaka M. Origin of the enantioselectivity of lipases explained by a stereo-sensing mechanism operative at the transition state. Bull Chem Soc Jpn 71 (1998) 443-453
    • (1998) Bull Chem Soc Jpn , vol.71 , pp. 443-453
    • Ema, T.1    Kobayashi, J.2    Maeno, S.3    Sakai, T.4    Utaka, M.5
  • 11
    • 0038111983 scopus 로고    scopus 로고
    • Structural and energetic determinants for enantiopreference in kinetic resolution of lipases
    • Bocola M., Stubbs M.T., Sotriffer C., Hauer B., Friedrich T., Dittrich K., et al. Structural and energetic determinants for enantiopreference in kinetic resolution of lipases. Protein Eng 16 (2003) 319-322
    • (2003) Protein Eng , vol.16 , pp. 319-322
    • Bocola, M.1    Stubbs, M.T.2    Sotriffer, C.3    Hauer, B.4    Friedrich, T.5    Dittrich, K.6
  • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
    • Lo Y.C., Lin S.C., Shaw J.F., and Liaw Y.C. Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network. J Mol Biol 330 (2003) 539-551
    • (2003) J Mol Biol , vol.330 , pp. 539-551
    • Lo, Y.C.1    Lin, S.C.2    Shaw, J.F.3    Liaw, Y.C.4
  • 15
    • 12344333653 scopus 로고    scopus 로고
    • The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism
    • Dunn G., Montgomery M.G., Mohammed F., Coker A., Cooper J.B., Robertson T., et al. The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism. J Mol Biol 346 (2005) 253-265
    • (2005) J Mol Biol , vol.346 , pp. 253-265
    • Dunn, G.1    Montgomery, M.G.2    Mohammed, F.3    Coker, A.4    Cooper, J.B.5    Robertson, T.6
  • 17
    • 0032103791 scopus 로고    scopus 로고
    • Anatomy of lipase binding sites: the scissile fatty acid binding site
    • Pleiss J., Fischer M., and Schimid R.D. Anatomy of lipase binding sites: the scissile fatty acid binding site. Chem Phys Lipids 93 (1998) 67-80
    • (1998) Chem Phys Lipids , vol.93 , pp. 67-80
    • Pleiss, J.1    Fischer, M.2    Schimid, R.D.3
  • 18
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • Bornscheuer U.T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 26 (2002) 73-81
    • (2002) FEMS Microbiol Rev , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 19
    • 0033653715 scopus 로고    scopus 로고
    • What distinguishes an esterase from a lipase: a novel structural approach
    • Fojan P., Jonson P.H., Petersen M.T.N., and Petersen S.B. What distinguishes an esterase from a lipase: a novel structural approach. Biochimie 82 (2000) 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
  • 21
    • 0034027595 scopus 로고    scopus 로고
    • Computational genetics: finding protein function by nonhomology methods
    • Marcotte E.M. Computational genetics: finding protein function by nonhomology methods. Curr Opin Struct Biol 10 (2000) 359-365
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 359-365
    • Marcotte, E.M.1
  • 22
    • 0036843441 scopus 로고    scopus 로고
    • Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters
    • Palomo J.M., Fernandez-Lorente G., Mateo C., Ortiz C., Fernandez-Lafuente R., and Guisan J.M. Modulation of the enantioselectivity of lipases via controlled immobilization and medium engineering: hydrolytic resolution of mandelic acid esters. Enzyme Microb Tech 31 (2002) 775-783
    • (2002) Enzyme Microb Tech , vol.31 , pp. 775-783
    • Palomo, J.M.1    Fernandez-Lorente, G.2    Mateo, C.3    Ortiz, C.4    Fernandez-Lafuente, R.5    Guisan, J.M.6
  • 23
    • 33645620298 scopus 로고    scopus 로고
    • Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Chung Y.M., Park C.B., and Lee S.B. Partial purification and characterization of thermostable esterase from the hyperthermophilic archaeon Sulfolobus solfataricus. Biotechnol Bioprocess Eng 5 (2000) 53-56
    • (2000) Biotechnol Bioprocess Eng , vol.5 , pp. 53-56
    • Chung, Y.M.1    Park, C.B.2    Lee, S.B.3
  • 24
    • 23644438017 scopus 로고    scopus 로고
    • Trichosporon beigelli esterase (TBE): a versatile esterase for the resolution of economically important racemates
    • Koul S., Koul J.L., Singh B., Kapoor M., Parshad R., Manhas K.S., et al. Trichosporon beigelli esterase (TBE): a versatile esterase for the resolution of economically important racemates. Tetrahedron: Asymmetry 16 (2005) 2575-2591
    • (2005) Tetrahedron: Asymmetry , vol.16 , pp. 2575-2591
    • Koul, S.1    Koul, J.L.2    Singh, B.3    Kapoor, M.4    Parshad, R.5    Manhas, K.S.6
  • 25
    • 33751499686 scopus 로고
    • A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa
    • Kazlauskas R.J., Weissfloch A.N.E., Rappaport A.T., and Cuccia L.A. A rule to predict which enantiomer of a secondary alcohol reacts faster in reactions catalyzed by cholesterol esterase, lipase from Pseudomonas cepacia, and lipase from Candida rugosa. J Org Chem 56 (1991) 2656-2665
    • (1991) J Org Chem , vol.56 , pp. 2656-2665
    • Kazlauskas, R.J.1    Weissfloch, A.N.E.2    Rappaport, A.T.3    Cuccia, L.A.4
  • 26
    • 0026014628 scopus 로고
    • Resolution of secondary alcohols by enzyme-catalyzed transesterification in alkyl carboxylates as the solvent
    • Janssen A.J.M., Klunder A.J.H., and Zwanenburg B. Resolution of secondary alcohols by enzyme-catalyzed transesterification in alkyl carboxylates as the solvent. Tetrahedron 47 (1991) 7645-7662
    • (1991) Tetrahedron , vol.47 , pp. 7645-7662
    • Janssen, A.J.M.1    Klunder, A.J.H.2    Zwanenburg, B.3
  • 27
    • 0031965757 scopus 로고    scopus 로고
    • Chiral recognition of alcohol enantiomers in acyl transfer reactions catalysed by Candida antarctica lipase B
    • Orrenius C., Hbffner F., Rotticci D., Öhrner N., Norin T., and Hult K. Chiral recognition of alcohol enantiomers in acyl transfer reactions catalysed by Candida antarctica lipase B. Biocatal Biotransform 16 (1998) 1-15
    • (1998) Biocatal Biotransform , vol.16 , pp. 1-15
    • Orrenius, C.1    Hbffner, F.2    Rotticci, D.3    Öhrner, N.4    Norin, T.5    Hult, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.