메뉴 건너뛰기




Volumn 54, Issue 3, 2007, Pages 230-236

EstA from Arthrobacter nitroguajacolicus Rü61a, a thermo- and solvent-tolerant carboxylesterase related to class C β-lactamases

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CARBOXYLESTERASE; SOLVENT;

EID: 33847152055     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-006-0438-2     Document Type: Article
Times cited : (31)

References (30)
  • 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
  • 2
    • 0036121221 scopus 로고    scopus 로고
    • Structural milestones in the reaction pathway of an amide hydrolase: Substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase
    • Beadle BM, Trehan I, Focia PJ, Shoichet BK (2002) Structural milestones in the reaction pathway of an amide hydrolase: Substrate, acyl, and product complexes of cephalothin with AmpC β-lactamase. Structure 10:413-424
    • (2002) Structure , vol.10 , pp. 413-424
    • Beadle, B.M.1    Trehan, I.2    Focia, P.J.3    Shoichet, B.K.4
  • 3
    • 0031726827 scopus 로고    scopus 로고
    • Molecular analysis of a gene encoding a cell-bound esterase from Streptomyces chrysomallus
    • Berger R, Hoffmann M, Keller U (1998) Molecular analysis of a gene encoding a cell-bound esterase from Streptomyces chrysomallus. J Bacteriol 180:6396-6399
    • (1998) J Bacteriol , vol.180 , pp. 6396-6399
    • Berger, R.1    Hoffmann, M.2    Keller, U.3
  • 4
    • 0027162890 scopus 로고
    • A dramatic change in the rate-limiting step of β-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C β-lactamase of Enterobacter cloacae 908R
    • Dubus A, Monnaie D, Jacobs C, Normark S, Frère JM (1993) A dramatic change in the rate-limiting step of β-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C β-lactamase of Enterobacter cloacae 908R. Biochem J 292:537-543
    • (1993) Biochem J , vol.292 , pp. 537-543
    • Dubus, A.1    Monnaie, D.2    Jacobs, C.3    Normark, S.4    Frère, J.M.5
  • 5
    • 0029068208 scopus 로고
    • Role of asparagine 152 in catalysis of β-lactam hydrolysis by Escherichia coli AmpC β-lactamase studied by site-directed mutagenesis
    • Dubus A, Normark S, Kania M, Page MGP (1995) Role of asparagine 152 in catalysis of β-lactam hydrolysis by Escherichia coli AmpC β-lactamase studied by site-directed mutagenesis. Biochemistry 34:7757-7764
    • (1995) Biochemistry , vol.34 , pp. 7757-7764
    • Dubus, A.1    Normark, S.2    Kania, M.3    Page, M.G.P.4
  • 6
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant SGN, Jessee J, Bloom FR, Hanahan D (1990) Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc Natl Acad Sci USA 87:4645-4649
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4645-4649
    • Grant, S.G.N.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 7
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D (1983) Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166:557-580
    • (1983) J Mol Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 8
    • 0031906319 scopus 로고    scopus 로고
    • A colorimetric assay for detecting haloalkane dehalogenase activity
    • Holloway P, Trevors JT, Lee H (1998) A colorimetric assay for detecting haloalkane dehalogenase activity. J Microbiol Methods 32:31-36
    • (1998) J Microbiol Methods , vol.32 , pp. 31-36
    • Holloway, P.1    Trevors, J.T.2    Lee, H.3
  • 9
    • 85007980736 scopus 로고
    • Cloning of Pseudomonas fluorescens carboxylesterase gene and characterization of its product expressed in Escherichia coli
    • Kim YS, Lee HB, Choi KD, Park S, Yoo OJ (1994) Cloning of Pseudomonas fluorescens carboxylesterase gene and characterization of its product expressed in Escherichia coli. Biosci Biotech Biochem 58:111-116
    • (1994) Biosci Biotech Biochem , vol.58 , pp. 111-116
    • Kim, Y.S.1    Lee, H.B.2    Choi, K.D.3    Park, S.4    Yoo, O.J.5
  • 10
    • 0035682334 scopus 로고    scopus 로고
    • Cloning and characterization of a gene cluster for cyclododecanone oxidation in Rhodococcus ruber SC1
    • Kostichka K, Thomas SM, Gibson KJ, Nagarajan V, Cheng Q (2001) Cloning and characterization of a gene cluster for cyclododecanone oxidation in Rhodococcus ruber SC1. J Bacteriol 183:6478-6486
    • (2001) J Bacteriol , vol.183 , pp. 6478-6486
    • Kostichka, K.1    Thomas, S.M.2    Gibson, K.J.3    Nagarajan, V.4    Cheng, Q.5
  • 11
    • 0023385987 scopus 로고
    • Rules for optimization of biocatalysis in organic solvents
    • Laane C, Boeren S, Vos K, Veeger C (1987) Rules for optimization of biocatalysis in organic solvents. Biotechnol Bioeng 30:81-87
    • (1987) Biotechnol Bioeng , vol.30 , pp. 81-87
    • Laane, C.1    Boeren, S.2    Vos, K.3    Veeger, C.4
  • 12
    • 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
  • 13
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky E, Moews PC, Liu H, Zhao H, Frère JM, Knox JR (1993) Evolution of an enzyme activity: Crystallographic structure at 2-Å resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc Natl Acad Sci USA 90:11257-11261
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frère, J.M.5    Knox, J.R.6
  • 14
    • 3242887157 scopus 로고    scopus 로고
    • CD-Search: Protein domain annotations on the fly
    • Marchler-Bauer A, Bryant SH (2004) CD-Search: Protein domain annotations on the fly. Nucleic Acids Res 32:W327-W331
    • (2004) Nucleic Acids Res , vol.32
    • Marchler-Bauer, A.1    Bryant, S.H.2
  • 16
    • 0000049351 scopus 로고
    • Purification and some properties of carboxylesterase from Arthrobacter globiformis: Stereoselective hydrolysis of ethyl chrysanthemate
    • Nishizawa M, Gomi H, Kishimoto F (1993) Purification and some properties of carboxylesterase from Arthrobacter globiformis: Stereoselective hydrolysis of ethyl chrysanthemate. Biosci Biotech Biochem 57:594-598
    • (1993) Biosci Biotech Biochem , vol.57 , pp. 594-598
    • Nishizawa, M.1    Gomi, H.2    Kishimoto, F.3
  • 17
    • 0029123341 scopus 로고
    • Stereoselective production of (+)-trans-chrysanthemic acid by a microbial esterase: Cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli
    • Nishizawa M, Shimizu M, Ohkawa H, Kanaoka M (1995) Stereoselective production of (+)-trans-chrysanthemic acid by a microbial esterase: Cloning, nucleotide sequence, and overexpression of the esterase gene of Arthrobacter globiformis in Escherichia coli. Appl Environ Microbiol 61:3208-3215
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3208-3215
    • Nishizawa, M.1    Shimizu, M.2    Ohkawa, H.3    Kanaoka, M.4
  • 19
    • 0035108407 scopus 로고    scopus 로고
    • Enzymes which are stable in the presence of organic solvents
    • Ogino H, Ishikawa H (2001) Enzymes which are stable in the presence of organic solvents. J Biosci Bioeng 91:109-116
    • (2001) J Biosci Bioeng , vol.91 , pp. 109-116
    • Ogino, H.1    Ishikawa, H.2
  • 22
    • 14044270156 scopus 로고    scopus 로고
    • Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate
    • Overhage J, Sielker S, Homburg S, Parschat K, Fetzner S (2005) Identification of large linear plasmids in Arthrobacter spp. encoding the degradation of quinaldine to anthranilate. Microbiology 151:491-500
    • (2005) Microbiology , vol.151 , pp. 491-500
    • Overhage, J.1    Sielker, S.2    Homburg, S.3    Parschat, K.4    Fetzner, S.5
  • 23
    • 0041344709 scopus 로고    scopus 로고
    • Gene cluster of Arthrobacter ilicis Rü61a involved in the degradation of quinaldine to anthranilate: Characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes
    • Parschat K, Hauer B, Kappl R, Kraft R, Hüttermann J, Fetzner S (2003) Gene cluster of Arthrobacter ilicis Rü61a involved in the degradation of quinaldine to anthranilate: Characterization and functional expression of the quinaldine 4-oxidase qoxLMS genes. J Biol Chem 278:27483-27494
    • (2003) J Biol Chem , vol.278 , pp. 27483-27494
    • Parschat, K.1    Hauer, B.2    Kappl, R.3    Kraft, R.4    Hüttermann, J.5    Fetzner, S.6
  • 24
    • 0035954552 scopus 로고    scopus 로고
    • A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to β-lactamases and DD-peptidases
    • Petersen EI, Valinger G, Sölkner B, Stubenrauch G, Schwab H (2001) A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to β-lactamases and DD-peptidases. J Biotechnol 89:11-25
    • (2001) J Biotechnol , vol.89 , pp. 11-25
    • Petersen, E.I.1    Valinger, G.2    Sölkner, B.3    Stubenrauch, G.4    Schwab, H.5
  • 25
    • 0029799968 scopus 로고    scopus 로고
    • The genus Nocardiopsis represents a phylogenetically coherent taxon and a distinct actinomycete lineage: Proposal of Nocardiopsaceae fam. nov
    • Rainey FA, Ward-Rainey N, Kroppenstedt RM, Stackebrandt E (1996) The genus Nocardiopsis represents a phylogenetically coherent taxon and a distinct actinomycete lineage: Proposal of Nocardiopsaceae fam. nov. Int J Syst Bacteriol 46:1088-1092
    • (1996) Int J Syst Bacteriol , vol.46 , pp. 1088-1092
    • Rainey, F.A.1    Ward-Rainey, N.2    Kroppenstedt, R.M.3    Stackebrandt, E.4
  • 28
    • 0035838468 scopus 로고    scopus 로고
    • Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site
    • Trehan I, Beadle BM, Shoichet BK (2001) Inhibition of AmpC β-lactamase through a destabilizing interaction in the active site. Biochemistry 40:7992-7999
    • (2001) Biochemistry , vol.40 , pp. 7992-7999
    • Trehan, I.1    Beadle, B.M.2    Shoichet, B.K.3
  • 29
    • 0036180211 scopus 로고    scopus 로고
    • EstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activity
    • Wagner UG, Petersen EI, Schwab H, Kratky C (2002) EstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activity. Protein Sci 11:467-478
    • (2002) Protein Sci , vol.11 , pp. 467-478
    • Wagner, U.G.1    Petersen, E.I.2    Schwab, H.3    Kratky, C.4
  • 30
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor T, Selinger Z (1996) Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies. Anal Biochem 236:302-308
    • (1996) Anal Biochem , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.