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Volumn 586, Issue 23, 2012, Pages 4186-4189

Crossover inhibition as an indicator of convergent evolution of enzyme mechanisms: A β-lactamase and a N-terminal nucleophile hydrolase

Author keywords

Lactamase; Convergent evolution; Enzyme; Inhibitors; Proteasome

Indexed keywords

1,3,4 OXATHIAZOL 2 ONE DERIVATIVE; AMINO TERMINAL TELOPEPTIDE; BETA LACTAMASE; BETA LACTAMASE INHIBITOR; HYDROLASE; O ARYLOXYCARBONYL HYDROXYMATE DERIVATIVE; PROTEASOME; UNCLASSIFIED DRUG;

EID: 84869498256     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.10.019     Document Type: Article
Times cited : (8)

References (23)
  • 2
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta-lactamase inhibitors
    • S.R. Drawz, and R.A. Bonomo Three decades of beta-lactamase inhibitors Clin. Microbiol. Rev. 1 2009 160 201
    • (2009) Clin. Microbiol. Rev. , vol.1 , pp. 160-201
    • Drawz, S.R.1    Bonomo, R.A.2
  • 3
    • 34547780834 scopus 로고    scopus 로고
    • O-Aryloxycarbonyl hydroxamates: New β-lactamase inhibitors that cross-link the active site
    • P.N. Wyrembak, K. Babaoglu, R.B. Pelto, B.K. Shoichet, and R.F. Pratt O-Aryloxycarbonyl hydroxamates: new β-lactamase inhibitors that cross-link the active site J. Am. Chem. Soc. 129 2007 9548 9549
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 9548-9549
    • Wyrembak, P.N.1    Babaoglu, K.2    Pelto, R.B.3    Shoichet, B.K.4    Pratt, R.F.5
  • 4
    • 56249115886 scopus 로고    scopus 로고
    • Kinetics and mechanism of inhibition of a serine β-lactamase by O-aryloxycarbonyl hydroxamates
    • R.B. Pelto, and R.F. Pratt Kinetics and mechanism of inhibition of a serine β-lactamase by O-aryloxycarbonyl hydroxamates Biochemistry 47 2008 12037 12046
    • (2008) Biochemistry , vol.47 , pp. 12037-12046
    • Pelto, R.B.1    Pratt, R.F.2
  • 5
    • 33947659939 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • L. Borissenko, and M. Groll 20S proteasome and its inhibitors: crystallographic knowledge for drug development Chem. Rev. 107 2007 687 717
    • (2007) Chem. Rev. , vol.107 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 7
    • 33645053287 scopus 로고    scopus 로고
    • Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate
    • G. Hu, G. Lin, M. Wang, L. Dick, R.-M. Xu, C. Nathan, and H. Li Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate Mol. Microbiol. 59 2006 1417 1428
    • (2006) Mol. Microbiol. , vol.59 , pp. 1417-1428
    • Hu, G.1    Lin, G.2    Wang, M.3    Dick, L.4    Xu, R.-M.5    Nathan, C.6    Li, H.7
  • 9
    • 0028806595 scopus 로고
    • The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution
    • J.A. Kelly, and A.P. Kuzin The refined crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 Å resolution J. Mol. Biol. 254 1995 233 236
    • (1995) J. Mol. Biol. , vol.254 , pp. 233-236
    • Kelly, J.A.1    Kuzin, A.P.2
  • 11
    • 0033082703 scopus 로고    scopus 로고
    • The β-lactamase cycle: A tale of selective pressure and bacterial ingenuity
    • A. Matagne, A. Dubus, M. Galleni, and J.-M. Frére The β-lactamase cycle: a tale of selective pressure and bacterial ingenuity Nat. Prod. Rep. 16 1999 1 19
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 1-19
    • Matagne, A.1    Dubus, A.2    Galleni, M.3    Frére, J.-M.4
  • 12
    • 53549099928 scopus 로고    scopus 로고
    • Evolution of class C β-lactamases: Factors influencing their hydrolysis and recognition mechanism
    • C. Fernollar-Ferrer, J. Frau, J. Donoso, and F. Munoz Evolution of class C β-lactamases: factors influencing their hydrolysis and recognition mechanism Theor. Chem. Acc. 121 2008 209 218
    • (2008) Theor. Chem. Acc. , vol.121 , pp. 209-218
    • Fernollar-Ferrer, C.1    Frau, J.2    Donoso, J.3    Munoz, F.4
  • 13
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • E. Sauvage, F. Kerff, M. Terrak, J.A. Ayala, and P. Charlier The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis FEMS Microbiol. Rev. 32 2008 234 258
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 14
    • 77955041712 scopus 로고    scopus 로고
    • Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: Interpretation of a transition state analogue in terms of catalytic mechanism
    • L. Dzhekieva, M. Rocaboy, F. Kerff, P. Charlier, E. Sauvage, and R.F. Pratt Crystal structure of a complex between the Actinomadura R39 DD-peptidase and a peptidoglycan-mimetic boronate inhibitor: interpretation of a transition state analogue in terms of catalytic mechanism Biochemistry 49 2010 6411 6419
    • (2010) Biochemistry , vol.49 , pp. 6411-6419
    • Dzhekieva, L.1    Rocaboy, M.2    Kerff, F.3    Charlier, P.4    Sauvage, E.5    Pratt, R.F.6
  • 16
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparisons of Ntn-hydrolases
    • C. Oinonen, and J. Rouvinen Structural comparisons of Ntn-hydrolases Protein Sci. 2 2000 2329 2337
    • (2000) Protein Sci. , vol.2 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 17
    • 84855290528 scopus 로고    scopus 로고
    • Divergence and convergence in enzyme evolution
    • G.Y. Galperin, and E.V. Koonin Divergence and convergence in enzyme evolution J. Biol. Chem. 287 2012 21 28
    • (2012) J. Biol. Chem. , vol.287 , pp. 21-28
    • Galperin, G.Y.1    Koonin, E.V.2
  • 18
    • 0031736387 scopus 로고    scopus 로고
    • Multimodular penicillin-binding proteins: An enigmatic family of orthologs and paralogs
    • C. Goffin, and J.-M. Ghuysen Multimodular penicillin-binding proteins: an enigmatic family of orthologs and paralogs Microbiol. Mol. Biol. Rev. 62 1998 1079 1083
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 1079-1083
    • Goffin, C.1    Ghuysen, J.-M.2
  • 19
    • 78149418550 scopus 로고    scopus 로고
    • Structural relationship between the active sites of β-lactam- recognizing and amidase signature enzymes: Convergent evolution?
    • R.F. Pratt, and M.J. McLeish Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: convergent evolution? Biochemistry 49 2010 9688 9697
    • (2010) Biochemistry , vol.49 , pp. 9688-9697
    • Pratt, R.F.1    McLeish, M.J.2
  • 20
    • 33644845743 scopus 로고    scopus 로고
    • Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
    • M. Groll, C.R. Berkers, H.L. Ploegh, and H. Ovaa Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome Structure 14 2006 451 458
    • (2006) Structure , vol.14 , pp. 451-458
    • Groll, M.1    Berkers, C.R.2    Ploegh, H.L.3    Ovaa, H.4
  • 22
    • 0029912405 scopus 로고    scopus 로고
    • Peptide aldehyde complexes with wheat serine carboxypeptidase II: Implications for the catalytic mechanism and substrate specificity
    • T.A. Bullock, K. Breddam, and S.J. Remington Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificity J. Mol. Biol. 255 1996 714 725
    • (1996) J. Mol. Biol. , vol.255 , pp. 714-725
    • Bullock, T.A.1    Breddam, K.2    Remington, S.J.3
  • 23
    • 0032511889 scopus 로고    scopus 로고
    • Crystal structure of a bacterial signal complex with a β-lactam inhibitor
    • M. Paetzel, R.E. Dalbey, and N.C.G. Strynadka Crystal structure of a bacterial signal complex with a β-lactam inhibitor Nature 396 1998 186 190
    • (1998) Nature , vol.396 , pp. 186-190
    • Paetzel, M.1    Dalbey, R.E.2    Strynadka, N.C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.