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Volumn 588, Issue 7, 2014, Pages 1154-1160

Crystal structure analysis of EstA from Arthrobacter sp. Rue61a - An insight into catalytic promiscuity

Author keywords

Catalytic promiscuity; Crystal structure; Esterase; Steric hindrance; Lactamase

Indexed keywords

BETA LACTAM; BETA LACTAMASE; CARBOXYLESTERASE; ESTA PROTEIN; ESTB PROTEIN; ESTERASE; ESTU1 PROTEIN; UNCLASSIFIED DRUG;

EID: 84897064424     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2014.02.045     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0026433541 scopus 로고
    • The energetics of intramolecular reactions and enzyme catalysis
    • M.I. Page The energetics of intramolecular reactions and enzyme catalysis Philos. Trans. R. Soc. Lond. B Biol. Sci. 332 1991 149 156
    • (1991) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.332 , pp. 149-156
    • Page, M.I.1
  • 3
    • 0033214082 scopus 로고    scopus 로고
    • Bacterial lipolytic enzymes: Classification and properties
    • J.L. Arpigny, and K.-E. Jaeger 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
  • 5
    • 0000908299 scopus 로고
    • AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of β-lactamases of the penicillinase type
    • B. Jaurin, and T. Grundstrom AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of β-lactamases of the penicillinase type Proc. Natl. Acad. Sci. USA 78 1981 4897 4901
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4897-4901
    • Jaurin, B.1    Grundstrom, T.2
  • 6
    • 0023446033 scopus 로고
    • Precise insertion of antibiotic resistance determinants into Tn21-like transposons: Nucleotide sequence of the OXA-1 β-lactamase gene
    • M. Ouellette, L. Bissonnette, and P.H. Roy Precise insertion of antibiotic resistance determinants into Tn21-like transposons: nucleotide sequence of the OXA-1 β-lactamase gene Proc. Natl. Acad. Sci. USA 84 1987 7378 7382
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7378-7382
    • Ouellette, M.1    Bissonnette, L.2    Roy, P.H.3
  • 7
    • 0032032930 scopus 로고    scopus 로고
    • Catalytic properties of class A β-lactamases: Efficiency and diversity
    • A. Matagne, J. Lamotte-Brasseur, and J.M. Frère Catalytic properties of class A β-lactamases: efficiency and diversity Biochem. J. 330 Pt 2 1998 581 598
    • (1998) Biochem. J. , vol.330 , Issue.PART 2 , pp. 581-598
    • Matagne, A.1    Lamotte-Brasseur, J.2    Frère, J.M.3
  • 8
    • 76249109230 scopus 로고    scopus 로고
    • Identification of group specific motifs in β-lactamase family of proteins
    • R. Singh, A. Saxena, and H. Singh Identification of group specific motifs in β-lactamase family of proteins J. Biomed. Sci. 16 2009 109 115
    • (2009) J. Biomed. Sci. , vol.16 , pp. 109-115
    • Singh, R.1    Saxena, A.2    Singh, H.3
  • 9
    • 0041842502 scopus 로고    scopus 로고
    • Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis
    • S.D. Goldberg, W. Iannuccilli, T. Nguyen, J. Ju, and V.W. Cornish Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis Protein Sci. 12 2003 1633 1645
    • (2003) Protein Sci. , vol.12 , pp. 1633-1645
    • Goldberg, S.D.1    Iannuccilli, W.2    Nguyen, T.3    Ju, J.4    Cornish, V.W.5
  • 10
    • 33847152055 scopus 로고    scopus 로고
    • EstA from Arthrobacter nitroguajacolicus Rü61a, a thermo- and solvent-tolerant carboxylesterase related to class C β-lactamases
    • M. Schütte, and S. Fetzner EstA from Arthrobacter nitroguajacolicus Rü61a, a thermo- and solvent-tolerant carboxylesterase related to class C β-lactamases Curr. Microbiol. 54 2007 230 236
    • (2007) Curr. Microbiol. , vol.54 , pp. 230-236
    • Schütte, M.1    Fetzner, S.2
  • 11
    • 0001049825 scopus 로고
    • Microiodometric assay for penicillinase
    • R.P. Novick Microiodometric assay for penicillinase Biochem. J. 83 1962 236 240
    • (1962) Biochem. J. , vol.83 , pp. 236-240
    • Novick, R.P.1
  • 13
    • 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
    • E.I. Petersen, G. Valinger, B. Sölkner, G. Stubenrauch, and H. Schwab A novel esterase from Burkholderia gladioli which shows high deacetylation activity on cephalosporins is related to β-lactamases and dd-peptidases J. Biotechnol. 89 2001 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
  • 14
    • 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
    • E. Lobkovsky, P.C. Moews, H. Liu, H. Zhao, J.M. Frère, and J.R. Knox 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 1993 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
  • 15
    • 84866978298 scopus 로고    scopus 로고
    • Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a
    • H. Niewerth, J. Schuldes, K. Parschat, P. Kiefer, J.A. Vorholt, R. Daniel, and S. Fetzner Complete genome sequence and metabolic potential of the quinaldine-degrading bacterium Arthrobacter sp. Rue61a BMC Genomics 13 2012 534
    • (2012) BMC Genomics , vol.13 , pp. 534
    • Niewerth, H.1    Schuldes, J.2    Parschat, K.3    Kiefer, P.4    Vorholt, J.A.5    Daniel, R.6    Fetzner, S.7
  • 17
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: Space-group determination, scaling and intensity statistics
    • P.R. Evans An introduction to data reduction: space-group determination, scaling and intensity statistics Acta Crystallogr. D Biol. Crystallogr. 67 2011 282 292
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 22
    • 84897037071 scopus 로고    scopus 로고
    • Schrödinger Package, New York
    • L. Schrödinger, Schrödinger Package, New York, 2009.
    • (2009)
    • Schrödinger, L.1
  • 23
    • 0346962971 scopus 로고    scopus 로고
    • Structural interaction fingerprint (SIFt): A novel method for analyzing three-dimensional protein-ligand binding interactions
    • Z. Deng, C. Chuaqui, and J. Singh Structural interaction fingerprint (SIFt): a novel method for analyzing three-dimensional protein-ligand binding interactions J. Med. Chem. 47 2004 337 344
    • (2004) J. Med. Chem. , vol.47 , pp. 337-344
    • Deng, Z.1    Chuaqui, C.2    Singh, J.3
  • 25
    • 0028224698 scopus 로고
    • Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition-state analog
    • E. Lobkovsky, E.M. Billings, P.C. Moews, J. Rahil, R.F. Pratt, and J.R. Knox Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a β-lactamase transition-state analog Biochemistry 33 1994 6762 6772
    • (1994) Biochemistry , vol.33 , pp. 6762-6772
    • Lobkovsky, E.1    Billings, E.M.2    Moews, P.C.3    Rahil, J.4    Pratt, R.F.5    Knox, J.R.6
  • 27
    • 0025027315 scopus 로고
    • Function of the conserved triad residues in the class C β-lactamase from Citrobacter freundii GN346
    • K. Tsukamoto, N. Nishida, M. Tsuruoka, and T. Sawai Function of the conserved triad residues in the class C β-lactamase from Citrobacter freundii GN346 FEBS Lett. 271 1990 243 246
    • (1990) FEBS Lett. , vol.271 , pp. 243-246
    • Tsukamoto, K.1    Nishida, N.2    Tsuruoka, M.3    Sawai, T.4
  • 29
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • T. Kawabata MATRAS: a program for protein 3D structure comparison Nucleic Acids Res. 31 2003 3367 3369
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3367-3369
    • Kawabata, T.1
  • 30
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • H. Ashkenazy, E. Erez, E. Martz, T. Pupko, and N. Ben-Tal ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids Nucleic Acids Res. 38 2010 W529 533
    • (2010) Nucleic Acids Res. , vol.38 , pp. 529-533
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 31
    • 57049150788 scopus 로고    scopus 로고
    • The ConSurf-DB: Pre-calculated evolutionary conservation profiles of protein structures
    • O. Goldenberg, E. Erez, G. Nimrod, and N. Ben-Tal The ConSurf-DB: pre-calculated evolutionary conservation profiles of protein structures Nucleic Acids Res. 37 2009 D323 327
    • (2009) Nucleic Acids Res. , vol.37 , pp. 323-327
    • Goldenberg, O.1    Erez, E.2    Nimrod, G.3    Ben-Tal, N.4
  • 34
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, and J. Liang CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 2006 W116 118
    • (2006) Nucleic Acids Res. , vol.34 , pp. 116-118
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 37
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, and K. Henrick Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions Acta Crystallogr. D Biol. Crystallogr. 60 2004 2256 2268
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 0029644940 scopus 로고
    • Where freedom is given, liberties are taken
    • G.J. Kleywegt, and T.A. Jones Where freedom is given, liberties are taken Structure 3 1995 535 540
    • (1995) Structure , vol.3 , pp. 535-540
    • Kleywegt, G.J.1    Jones, T.A.2


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