158 related articles for article (PubMed ID: 11847294)
1. Functional control of the binuclear metal site in the metallo-beta-lactamase-like fold by subtle amino acid replacements.
Gomes CM; Frazão C; Xavier AV; Legall J; Teixeira M
Protein Sci; 2002 Mar; 11(3):707-12. PubMed ID: 11847294
[TBL] [Abstract][Full Text] [Related]
2. Identification of metal binding residues for the binuclear zinc phosphodiesterase reveals identical coordination as glyoxalase II.
Vogel A; Schilling O; Meyer-Klaucke W
Biochemistry; 2004 Aug; 43(32):10379-86. PubMed ID: 15301536
[TBL] [Abstract][Full Text] [Related]
3. Flexible metal binding of the metallo-beta-lactamase domain: glyoxalase II incorporates iron, manganese, and zinc in vivo.
Schilling O; Wenzel N; Naylor M; Vogel A; Crowder M; Makaroff C; Meyer-Klaucke W
Biochemistry; 2003 Oct; 42(40):11777-86. PubMed ID: 14529289
[TBL] [Abstract][Full Text] [Related]
4. Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.
Rasia RM; Ceolín M; Vila AJ
Protein Sci; 2003 Jul; 12(7):1538-46. PubMed ID: 12824499
[TBL] [Abstract][Full Text] [Related]
5. Structural consequences of the active site substitution Cys181 ==> Ser in metallo-beta-lactamase from Bacteroides fragilis.
Li Z; Rasmussen BA; Herzberg O
Protein Sci; 1999 Jan; 8(1):249-52. PubMed ID: 10210203
[TBL] [Abstract][Full Text] [Related]
6. Biochemical and structural characterization of Salmonella typhimurium glyoxalase II: new insights into metal ion selectivity.
Campos-Bermudez VA; Leite NR; Krog R; Costa-Filho AJ; Soncini FC; Oliva G; Vila AJ
Biochemistry; 2007 Oct; 46(39):11069-79. PubMed ID: 17764159
[TBL] [Abstract][Full Text] [Related]
7. Bulgecin A: a novel inhibitor of binuclear metallo-beta-lactamases.
Simm AM; Loveridge EJ; Crosby J; Avison MB; Walsh TR; Bennett PM
Biochem J; 2005 May; 387(Pt 3):585-90. PubMed ID: 15569001
[TBL] [Abstract][Full Text] [Related]
8. Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme.
Fabiane SM; Sohi MK; Wan T; Payne DJ; Bateson JH; Mitchell T; Sutton BJ
Biochemistry; 1998 Sep; 37(36):12404-11. PubMed ID: 9730812
[TBL] [Abstract][Full Text] [Related]
9. Crystal structures of the cadmium- and mercury-substituted metallo-beta-lactamase from Bacteroides fragilis.
Concha NO; Rasmussen BA; Bush K; Herzberg O
Protein Sci; 1997 Dec; 6(12):2671-6. PubMed ID: 9416622
[TBL] [Abstract][Full Text] [Related]
10. Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
González JM; Buschiazzo A; Vila AJ
Biochemistry; 2010 Sep; 49(36):7930-8. PubMed ID: 20677753
[TBL] [Abstract][Full Text] [Related]
11. Design and evolution of new catalytic activity with an existing protein scaffold.
Park HS; Nam SH; Lee JK; Yoon CN; Mannervik B; Benkovic SJ; Kim HS
Science; 2006 Jan; 311(5760):535-8. PubMed ID: 16439663
[TBL] [Abstract][Full Text] [Related]
12. Spectroscopic characterization of a binuclear metal site in Bacillus cereus beta-lactamase II.
Orellano EG; Girardini JE; Cricco JA; Ceccarelli EA; Vila AJ
Biochemistry; 1998 Jul; 37(28):10173-80. PubMed ID: 9665723
[TBL] [Abstract][Full Text] [Related]
13. Metal content and localization during turnover in B. cereus metallo-beta-lactamase.
Llarrull LI; Tioni MF; Vila AJ
J Am Chem Soc; 2008 Nov; 130(47):15842-51. PubMed ID: 18980306
[TBL] [Abstract][Full Text] [Related]
14. Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis.
Concha NO; Rasmussen BA; Bush K; Herzberg O
Structure; 1996 Jul; 4(7):823-36. PubMed ID: 8805566
[TBL] [Abstract][Full Text] [Related]
15. The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution.
Ullah JH; Walsh TR; Taylor IA; Emery DC; Verma CS; Gamblin SJ; Spencer J
J Mol Biol; 1998 Nov; 284(1):125-36. PubMed ID: 9811546
[TBL] [Abstract][Full Text] [Related]
16. Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis.
Crowder MW; Wang Z; Franklin SL; Zovinka EP; Benkovic SJ
Biochemistry; 1996 Sep; 35(37):12126-32. PubMed ID: 8810919
[TBL] [Abstract][Full Text] [Related]
17. Protonation state of Asp120 in the binuclear active site of the metallo-beta-lactamase from Bacteroides fragilis.
Dal Peraro M; Vila AJ; Carloni P
Inorg Chem; 2003 Jul; 42(14):4245-7. PubMed ID: 12844290
[TBL] [Abstract][Full Text] [Related]
18. An evolutionary classification of the metallo-beta-lactamase fold proteins.
Aravind L
In Silico Biol; 1999; 1(2):69-91. PubMed ID: 11471246
[TBL] [Abstract][Full Text] [Related]
19. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism.
Davies AM; Rasia RM; Vila AJ; Sutton BJ; Fabiane SM
Biochemistry; 2005 Mar; 44(12):4841-9. PubMed ID: 15779910
[TBL] [Abstract][Full Text] [Related]
20. Positively cooperative binding of zinc ions to Bacillus cereus 569/H/9 beta-lactamase II suggests that the binuclear enzyme is the only relevant form for catalysis.
Jacquin O; Balbeur D; Damblon C; Marchot P; De Pauw E; Roberts GC; Frère JM; Matagne A
J Mol Biol; 2009 Oct; 392(5):1278-91. PubMed ID: 19665032
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
