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Volumn 81, Issue 11, 2013, Pages 2045-2051

Structural basis for the β-lactamase activity of EstU1, a family VIII carboxylesterase

Author keywords

lactamase activity; Crystal structure of EstU1; Crystal structure of the EstU1 cephalothin complex; EstU1; Family VIII carboxylesterases

Indexed keywords

BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; CARBOXYLESTERASE; CEFALOTIN;

EID: 84885796337     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24334     Document Type: Article
Times cited : (35)

References (27)
  • 1
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • Bornscheuer UT. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol Rev 2002;26(1):73-81.
    • (2002) FEMS Microbiol Rev , vol.26 , Issue.1 , pp. 73-81
    • Bornscheuer, U.T.1
  • 2
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: the family keeps growing
    • Nardini M, Dijkstra BW. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr Opin Struct Biol 1999;9(6):732-737.
    • (1999) Curr Opin Struct Biol , vol.9 , Issue.6 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2
  • 3
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • Jaeger KE, Dijkstra BW, Reetz MT. Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases. Annu Rev Microbiol 1999;53:315-351.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 6
    • 0035725911 scopus 로고    scopus 로고
    • Production, purification, characterization, and applications of lipases
    • Sharma R, Chisti Y, Banerjee UC. Production, purification, characterization, and applications of lipases. Biotechnol Adv 2001;19(8):627-662.
    • (2001) Biotechnol Adv , vol.19 , Issue.8 , pp. 627-662
    • Sharma, R.1    Chisti, Y.2    Banerjee, U.C.3
  • 7
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: classification and properties
    • Arpigny JL, Jaeger KE. Bacterial lipolytic enzymes: classification and properties. Biochem J 1999;343(Pt 1):177-183.
    • (1999) Biochem J , vol.343 , Issue.PART 1 , pp. 177-183
    • Arpigny, J.L.1    Jaeger, K.E.2
  • 8
    • 0036180211 scopus 로고    scopus 로고
    • EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity
    • Wagner UG, Petersen EI, Schwab H, Kratky C. EstB from Burkholderia gladioli: a novel esterase with a beta-lactamase fold reveals steric factors to discriminate between esterolytic and beta-lactam cleaving activity. Protein Sci 2002;11(3):467-478.
    • (2002) Protein Sci , vol.11 , Issue.3 , pp. 467-478
    • Wagner, U.G.1    Petersen, E.I.2    Schwab, H.3    Kratky, C.4
  • 9
    • 0035954552 scopus 로고    scopus 로고
    • A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to beta-lactamases and DD-peptidases
    • Petersen EI, Valinger G, Solkner B, Stubenrauch G, Schwab H. A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to beta-lactamases and DD-peptidases. J Biotechnol 2001;89(1):11-25.
    • (2001) J Biotechnol , vol.89 , Issue.1 , pp. 11-25
    • Petersen, E.I.1    Valinger, G.2    Solkner, B.3    Stubenrauch, G.4    Schwab, H.5
  • 10
    • 67349147516 scopus 로고    scopus 로고
    • A novel family VIII carboxylesterase derived from a leachate metagenome library exhibits promiscuous beta-lactamase activity on nitrocefin
    • Rashamuse K, Magomani V, Ronneburg T, Brady D. A novel family VIII carboxylesterase derived from a leachate metagenome library exhibits promiscuous beta-lactamase activity on nitrocefin. Appl Microbiol Biotechnol 2009;83(3):491-500.
    • (2009) Appl Microbiol Biotechnol , vol.83 , Issue.3 , pp. 491-500
    • Rashamuse, K.1    Magomani, V.2    Ronneburg, T.3    Brady, D.4
  • 12
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol 1997;276:307-326.
    • (1997) Method Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 13
    • 2142689200 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution, density modification and model building
    • Terwilliger T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J Synchrotron Radiat 2004;11(Pt 1):49-52.
    • (2004) J Synchrotron Radiat , vol.11 , Issue.PART 1 , pp. 49-52
    • Terwilliger, T.1
  • 15
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 17
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53(Pt 3):240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 19
    • 0037130228 scopus 로고    scopus 로고
    • Structure-based approach for binding site identification on AmpC beta-lactamase
    • Powers RA, Shoichet BK. Structure-based approach for binding site identification on AmpC beta-lactamase. J Med Chem 2002;45(15):3222-3234.
    • (2002) J Med Chem , vol.45 , Issue.15 , pp. 3222-3234
    • Powers, R.A.1    Shoichet, B.K.2
  • 20
    • 61449127371 scopus 로고    scopus 로고
    • Re-examining the role of Lys67 in class C beta-lactamase catalysis
    • Chen Y, McReynolds A, Shoichet BK. Re-examining the role of Lys67 in class C beta-lactamase catalysis. Protein Sci 2009;18(3):662-669.
    • (2009) Protein Sci , vol.18 , Issue.3 , pp. 662-669
    • Chen, Y.1    McReynolds, A.2    Shoichet, B.K.3
  • 22
    • 0035967506 scopus 로고    scopus 로고
    • Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone
    • Crichlow GV, Nukaga M, Doppalapudi VR, Buynak JD, Knox JR. Inhibition of class C beta-lactamases: structure of a reaction intermediate with a cephem sulfone. Biochemistry 2001;40(21):6233-6239.
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6233-6239
    • Crichlow, G.V.1    Nukaga, M.2    Doppalapudi, V.R.3    Buynak, J.D.4    Knox, J.R.5
  • 23
    • 0035822659 scopus 로고    scopus 로고
    • Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design
    • Powers RA, Caselli E, Focia PJ, Prati F, Shoichet BK. Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design. Biochemistry 2001;40(31):9207-9214.
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9207-9214
    • Powers, R.A.1    Caselli, E.2    Focia, P.J.3    Prati, F.4    Shoichet, B.K.5
  • 24
    • 0035838468 scopus 로고    scopus 로고
    • Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site
    • Trehan I, Beadle BM, Shoichet BK. Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site. Biochemistry 2001;40(27):7992-7999.
    • (2001) Biochemistry , vol.40 , Issue.27 , pp. 7992-7999
    • Trehan, I.1    Beadle, B.M.2    Shoichet, B.K.3
  • 25
    • 0036121221 scopus 로고    scopus 로고
    • Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase
    • Beadle BM, Trehan I, Focia PJ, Shoichet BK. Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase. Structure 2002;10(3):413-424.
    • (2002) Structure , vol.10 , Issue.3 , pp. 413-424
    • Beadle, B.M.1    Trehan, I.2    Focia, P.J.3    Shoichet, B.K.4
  • 26
    • 0024603697 scopus 로고
    • Effect of the 3′-leaving group on turnover of cephem antibiotics by a class C b-lactamase
    • Mazella J, Pratt RF. Effect of the 3′-leaving group on turnover of cephem antibiotics by a class C b-lactamase. Biochem J 1989;259:255-260.
    • (1989) Biochem J , vol.259 , pp. 255-260
    • Mazella, J.1    Pratt, R.F.2
  • 27
    • 1542274594 scopus 로고    scopus 로고
    • Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes
    • Nukaga M, Kumar S, Nukaga K, Pratt RF, Knox JR. Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes. J Biol Chem 2004;279(10):9344-9352.
    • (2004) J Biol Chem , vol.279 , Issue.10 , pp. 9344-9352
    • Nukaga, M.1    Kumar, S.2    Nukaga, K.3    Pratt, R.F.4    Knox, J.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.