IMP-1 metallo-β-lactamase: Effect of chelators and assessment of metal requirement by electrospray mass spectrometry

Biochimica et Biophysica Acta - General Subjects

Volumn 1571, Issue 3, 2002, Pages 190-200

  Siemann, Stefan ^a   Brewer, Dyanne ^b   Clarke, Anthony J ^c   Dmitrienko, Gary I ^a   Lajoie, Gilles ^b   Viswanatha, Thammaiah ^a  

^a UNIVERSITY OF WATERLOO   (Canada)

^b UNIVERSITY OF WESTERN ONTARIO   (Canada)

^c UNIVERSITY OF GUELPH   (Canada)

Author keywords

Antibiotic resistance; Chelator; Denaturation; Electrospray ionization mass spectrometry; Fluorescence; Metallo lactamase

Indexed keywords

4 (2 PYRIDYLAZO)RESORCINOL; BETA LACTAMASE; CHELATING AGENT; DIPICOLINIC ACID; ENZYME INHIBITOR; GUANIDINE; HOLOENZYME; METAL; METAL ION; PROTEIN; PROTEIN IMP 1; UNCLASSIFIED DRUG; ZINC;

ARTICLE; CATALYSIS; COMPLEX FORMATION; DENATURATION; ENZYME ANALYSIS; ENZYME ASSAY; ENZYME INACTIVATION; MASS SPECTROMETRY; PREVALENCE; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA;

BETA-LACTAMASES; CATALYSIS; CHELATING AGENTS; ENZYME ACTIVATION; ENZYME INHIBITORS; GUANIDINE; KINETICS; PSEUDOMONAS AERUGINOSA; RESORCINOLS; SPECTROMETRY, FLUORESCENCE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; ZINC;

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 0037014621     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(02)00258-1     Document Type: Article

References (53)

1. Penicillin resistance: The chemistry of β-lactamase inhibition
2. The β-lactamase cycle: A tale of selective pressure and bacterial ingenuity
3. The mechanism of catalysis and the inhibition of β-lactamases
4. Molecular mechanisms that confer antibacterial drug resistance
5. The structure of β-lactamases
6. Serine β-lactamases and penicillin-binding proteins
7. Metallo-β-lactamase: Structure and mechanism
8. Class B β-lactamases: The importance of being metallic
9. Zn(II) dependence of the Aeromonas hydrophila AE036 metallo-β-lactamase activity and stability
10. Characterization of the metal-binding sites of the β-lactamase from Bacteroides fragilis
11. Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-β-lactamase that provides multiple antibiotic resistance
12. Mono- and binuclear Zn-β-lactamase from Bacteroides fragilis: Catalytic and structural roles of the zinc ions
13. Spectroscopic characterization of a binuclear metal site in Bacillus cereus β-lactamase II
14. The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent β-lactamase
15. 2+-β-lactamase. Role of the conserved cysteine in the catalytic mechanism
16. On the mechanism of the metallo-β-lactamase from Bacteroides fragilis
17. Molecular dynamics simulations of the mononuclear zinc-β-lactamase from Bacillus cereus complexed with benzylpenicillin and a quantum chemical study of the reaction mechanism
18. Transferable imipenem resistance in Pseudomonas aeruginosa
19. IMP-containing Pseudomonas aeruginosa integron phyletically related to In5, which carries an unusual array of gene cassettes
20. Biochemical characterization of the Pseudomonas aeruginosa 101/1477 metallo-β-lactamase IMP-1 produced by Escherichia coli
21. Functional analysis of the active site of a metallo-β-lactamase proliferating in Japan
22. Cleavage of structural proteins during the assembly of the head of bacteriophage T4
23. Novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate
24. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase
25. The determination of enzyme inhibitor constants
26. Noncovalent associations of glutathione S-transferase and ligands: A study using electrospray quadrupole/time-of-flight mass spectrometry
27. Disentangling electrospray spectra with maximum entropy
28. Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-β-lactamase from Bacteroides fragilis
29. Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
30. Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein
31. Colorimetric determination of zinc and copper with 2-carboxy-2′-hydroxy-5′-sulfoformazylbenzene
32. Effect of high salt concentrations on water structure
33. Differential chemical reactivities of zinc in horse liver alcohol dehydrogenase
34. Kinetic properties and metal content of the metallo-β-lactamase CcrA harboring selective amino acid substitutions
35. Dynamic protein complexes: Insights from mass spectrometry
36. Biochemical characterization of the metallo-β-lactamase CcrA from Bacteroides fragilis TAL3636
37. Crystal structure of the wide-spectrum binuclear zinc β-lactamase from Bacteroides fragilis
38. Unanticipated inhibition of the metallo-β-lactamase from Bacteroides fragilis by 4-morpholineethanesulfonic acid (MES): A crystallographic study at 1.85-Å resolution
39. Molecular characterization of an enterobacterial metallo-β-lactamase found in clinical isolate of Serratia marcescens that shows imipenem resistance
40. Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: A new molecular class B β-lactamase showing a broad substrate profile
41. The production and molecular properties of the zinc β-lactamase of Pseudomonas maltophilia IID 1275
42. Biochemical characterization of the FEZ-1 metallo-β-lactamase of Legionella gormanii ATCC 33297T produced in Escherichia coli
43. Metal ion binding and coordination geometry for wild type and mutants of metallo-β-lactamase from Bacillus cereus 569/H/9 (BcII): A combined thermodynamic, kinetic, and spectroscopic approach
44. Exploring the role and the binding affinity of a second zinc equivalent in B. cereus metallo-β-lactamase
45. The Metallo-β-lactamase Working Group, standard numbering scheme for class B β-lactamases
46. The 3-D structure of a zinc metallo-β-lactamase from Bacillus cereus reveals a new type of protein fold
47. Crystal structure of the zinc-dependent β-lactamase from Bacillus cereus at 1.9 Å resolution: Binuclear active site with features of a mononuclear enzyme
48. Crystal structure of the IMP-1 metallo-β-lactamase from Pseudomonas aeruginosa and its complex with a mercaptocarboxylate inhibitor: Binding determinants of a potent, broad-spectrum inhibitor
49. Substrate-activated give binding of metallo-β-lactamases: Physiological importance of mononuclear enzymes