메뉴 건너뛰기




Volumn 88, Issue 7, 2006, Pages 859-867

Esterase EstA6 from Pseudomonas sp. CR-611 is a novel member in the utmost conserved cluster of family VI bacterial lipolytic enzymes

Author keywords

Bacterial lipase classification; Carboxylesterase; Pseudomonas

Indexed keywords

BACTERIAL ENZYME; BUTYRIC ACID; ENZYME ESTA6; ESTERASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 33746479149     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.02.011     Document Type: Article
Times cited : (19)

References (34)
  • 1
    • 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
  • 2
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: molecular biology, three-dimensional structure, and biotechnological applications of lipases
    • Jaeger K.E., Dijkstra B.W., and Reetz M.T. Bacterial biocatalysts: molecular biology, three-dimensional structure, and biotechnological applications of lipases. Annu. Rev. Microbiol. 53 (1999) 315-351
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 3
    • 3142773489 scopus 로고    scopus 로고
    • Bacterial lipases: an overview of production, purification and biochemical properties
    • Gupta R., Gupta N., and Rathi P. Bacterial lipases: an overview of production, purification and biochemical properties. Appl. Microbiol. Biotechnol. 64 (2004) 763-781
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 763-781
    • Gupta, R.1    Gupta, N.2    Rathi, P.3
  • 4
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • Khalameyzer V., Fischer I., Bornscheuer U.T., and Altenbuchner J. Screening, nucleotide sequence and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones. Appl. Environ. Microbiol. 65 (1999) 477-482
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 7
    • 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
  • 8
    • 0001603385 scopus 로고    scopus 로고
    • Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity
    • Kim K.K., Song H.K., Shin D.H., Hwang K.Y., Choe S., Yoo O.J., and Suh S.W. Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity. Structure 5 (1997) 1571-1584
    • (1997) Structure , vol.5 , pp. 1571-1584
    • Kim, K.K.1    Song, H.K.2    Shin, D.H.3    Hwang, K.Y.4    Choe, S.5    Yoo, O.J.6    Suh, S.W.7
  • 9
    • 0028198291 scopus 로고
    • Cloning and characterization of the gene encoding an esterase from Spirulina platensis
    • Salvi S., Trieni M., Lanfaloni L., and Pon C.L. Cloning and characterization of the gene encoding an esterase from Spirulina platensis. Mol. Gen. Genet. 243 (1994) 124-126
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 124-126
    • Salvi, S.1    Trieni, M.2    Lanfaloni, L.3    Pon, C.L.4
  • 11
    • 14644408029 scopus 로고    scopus 로고
    • Isolation of lipid- and polysaccharide-degrading microorganisms from subtropical forest soil, and analysis of lipolytic strain Bacillus sp. CR-179
    • Ruiz C., Pastor F.I.J., and Diaz P. Isolation of lipid- and polysaccharide-degrading microorganisms from subtropical forest soil, and analysis of lipolytic strain Bacillus sp. CR-179. Lett. Appl. Microbiol. 40 (2005) 218-227
    • (2005) Lett. Appl. Microbiol. , vol.40 , pp. 218-227
    • Ruiz, C.1    Pastor, F.I.J.2    Diaz, P.3
  • 12
    • 0023089142 scopus 로고
    • Specific and sensitive plate assay for bacterial lipases
    • Kouker G., and Jaeger K.E. Specific and sensitive plate assay for bacterial lipases. Appl. Environ. Microbiol. 53 (1987) 211-213
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 211-213
    • Kouker, G.1    Jaeger, K.E.2
  • 13
    • 0023811628 scopus 로고
    • Chromossomal mutations that increase the production of a plasmid encoded haemolysin in Escherichia coli
    • Godessart N., Muñoa F.J., Regué M., and Juárez A. Chromossomal mutations that increase the production of a plasmid encoded haemolysin in Escherichia coli. J. Gen. Microbiol. 134 (1988) 2779-2787
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 2779-2787
    • Godessart, N.1    Muñoa, F.J.2    Regué, M.3    Juárez, A.4
  • 16
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: signalP 3.0
    • Bendtsen J.D., Nielsen H., Heijne G., and Brunak S. Improved prediction of signal peptides: signalP 3.0. J. Mol. Biol. 340 (2004) 783-795
    • (2004) J. Mol. Biol. , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    Heijne, G.3    Brunak, S.4
  • 18
    • 0000732090 scopus 로고
    • Evolution of protein molecules
    • Munro H.N. (Ed), Academic Press, New york
    • Jukes T.H., and Cantor R.R. Evolution of protein molecules. In: Munro H.N. (Ed). Mammalian protein metabolism (1966), Academic Press, New york 21-132
    • (1966) Mammalian protein metabolism , pp. 21-132
    • Jukes, T.H.1    Cantor, R.R.2
  • 19
    • 0031604140 scopus 로고    scopus 로고
    • Phylogenetic inference in protein superfamilies: analysis of SH2 domains
    • Sjölander K. Phylogenetic inference in protein superfamilies: analysis of SH2 domains. Proc. Int. Conf. Intell. Syst. Mol. Biol. 6 (1998) 166-174
    • (1998) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.6 , pp. 166-174
    • Sjölander, K.1
  • 20
    • 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., Martínez J., Pastor F.I.J., and Diaz P. 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 (2000) 303-312
    • (2000) Res. Microbiol. , vol.151 , pp. 303-312
    • Prim, N.1    Blanco, A.2    Martínez, J.3    Pastor, F.I.J.4    Diaz, P.5
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0032869128 scopus 로고    scopus 로고
    • Direct fluorescence-based lipase activity assay
    • Diaz P., Prim N., and Pastor F.I.J. Direct fluorescence-based lipase activity assay. Biotechniques 27 (1999) 696-700
    • (1999) Biotechniques , vol.27 , pp. 696-700
    • Diaz, P.1    Prim, N.2    Pastor, F.I.J.3
  • 23
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids. Symp. Ser. 41 (1999) 95-98
    • (1999) Nucl. Acids. Symp. Ser. , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 24
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H., Engelbrecht J., Brunak S., and von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Prot. Eng. 10 (1997) 1-6
    • (1997) Prot. Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    von Heijne, G.4
  • 25
    • 0030759333 scopus 로고    scopus 로고
    • Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method
    • Cserzo M., Wallin E., Simon L., von Heijne G., and Elofsson A. Prediction of transmembrane alpha-helices in prokaryotic membrane proteins: the dense alignment surface method. Protein Eng. 10 (1997) 673-676
    • (1997) Protein Eng. , vol.10 , pp. 673-676
    • Cserzo, M.1    Wallin, E.2    Simon, L.3    von Heijne, G.4    Elofsson, A.5
  • 26
    • 15844431346 scopus 로고    scopus 로고
    • PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
    • Gardy J.L., Laird M.R., Chen F., Rey S., Walsh C.J., Ester M., and Brinkman F.S.L. PSORTb v.2.0: expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis. Bioinformatics 21 (2004) 617-623
    • (2004) Bioinformatics , vol.21 , pp. 617-623
    • Gardy, J.L.1    Laird, M.R.2    Chen, F.3    Rey, S.4    Walsh, C.J.5    Ester, M.6    Brinkman, F.S.L.7
  • 27
    • 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., Falcocchio S., Xoxi E., Pastor F.I.J., Diaz P., and Saso L. Activation and inhibition of Candida rugosa and Bacillus-related lipases by saturated fatty acids evaluated by a new colorimetric microassay. Biochim. Biophys. Acta 1672 (2004) 184-191
    • (2004) Biochim. Biophys. Acta , vol.1672 , pp. 184-191
    • Ruiz, C.1    Falcocchio, S.2    Xoxi, E.3    Pastor, F.I.J.4    Diaz, P.5    Saso, L.6
  • 28
    • 13444302764 scopus 로고    scopus 로고
    • Funshift: a database of function shift analysis on protein subfamilies
    • Abhiman S., and Sonnhammer E. Funshift: a database of function shift analysis on protein subfamilies. Nucleic Acids Res. 33 (2005) 197-200
    • (2005) Nucleic Acids Res. , vol.33 , pp. 197-200
    • Abhiman, S.1    Sonnhammer, E.2
  • 29
    • 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
  • 30
    • 0026250066 scopus 로고
    • Characterization of Pseudomonas fluorescens carboxylesterase: cloning and expression of the esterase gene in Escherichia coli
    • Hong K.H., Jang W.H., Choi K.D., and Yoo O.J. Characterization of Pseudomonas fluorescens carboxylesterase: cloning and expression of the esterase gene in Escherichia coli. Agric. Biol. Chem. 55 (1991) 2839-2845
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 2839-2845
    • Hong, K.H.1    Jang, W.H.2    Choi, K.D.3    Yoo, O.J.4
  • 31
    • 1642325863 scopus 로고    scopus 로고
    • Genome-wide cloning and characterization of microbial esterases
    • Ro H.S., Hong H.P., Kho B.H., Kim S., and Chung B.H. Genome-wide cloning and characterization of microbial esterases. FEMS Microbiol. Lett. 223 (2004) 97-105
    • (2004) FEMS Microbiol. Lett. , vol.223 , pp. 97-105
    • Ro, H.S.1    Hong, H.P.2    Kho, B.H.3    Kim, S.4    Chung, B.H.5
  • 33
    • 1242284208 scopus 로고    scopus 로고
    • Cold active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly > Pro substitution near the active site on its catalytic activity and stability
    • Kulakova L., Galkin A., Nakayama T., Nishino T., and Esaki N. Cold active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly > Pro substitution near the active site on its catalytic activity and stability. Biochim. Biophys. Acta 1629 (2004) 59-65
    • (2004) Biochim. Biophys. Acta , vol.1629 , pp. 59-65
    • Kulakova, L.1    Galkin, A.2    Nakayama, T.3    Nishino, T.4    Esaki, N.5
  • 34
    • 0035098789 scopus 로고    scopus 로고
    • Cloning and characterisation of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7
    • Prim N., Pastor F.I.J., and Diaz P. Cloning and characterisation of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7. Curr. Microbiol. 42 (2001) 237-240
    • (2001) Curr. Microbiol. , vol.42 , pp. 237-240
    • Prim, N.1    Pastor, F.I.J.2    Diaz, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.