| References: | 1. Fre`re, J. M. (1995) Beta-lactamases and bacterial resistance to
antibiotics, Mol. Microbiol. 16, 385-395.
2. Wang, Z., Fast, W., Valentine, A. M., and Benkovic, S. J. (1999)
Metallo-â-lactamase: structure and function, Curr. Opin. Chem.
Biol. 3, 614-622.
3. Laraki, N., Franceschini, N., Rossolini, G. M., Santucci, P.,
Meunier, C., de Pauw, E., Amicosante, G., Fre`re, J. M., and
Galleni, M. (1999) Biochemical characterisation of the Pseudomonas
aeruginosa 101/1477 metallo-â-lactamase IMP-1 produced
by Escherichia coli, Antimicrob. Agents Chemother. 43, 902-
906; Payne, D. J. (1993) Metallo-beta-lactamasessa new therapeutic
challenge, J. Med. Microbiol. 39, 93-99.
4. Galleni, M., Lamotte-Brasseur, J., Rossolini, G. M., Spencer, J.,
Dideberg, O., and Fre`re, J. M. (2001) Standard numbering scheme
for class B â-lactamases, Antimicrob. Agents Chemother. 45, 660-
663.
5. Fabiane, S. M., Sohi, M. K., Wan, T., Payne, D. J., Bateson, J.
H., Mitchell, T., and Sutton, B. J. (1998) Crystal structure of the
zinc-dependent â-lactamase from Bacillus cereus at 1.9 Å
resolution: binuclear active site with features of a mononuclear
enzyme, Biochemistry 37, 12404-12411.
6. Orellano, E. G., Girardini, J. E., Cricco, J. A., Ceccarelli, E. A.,
and Vila, A. J. (1998) Spectroscopic characterization of a binuclear
metal site in Bacillus cereus â-lactamase II, Biochemistry 37,
10173-10180; Paul-Soto, R., Bauer, R., Fre`re, J. M., Galleni,
M., Meyer-Klaucke, W., Nolting, H., Rossolini, G. M., de Seny,
D., Hernandez-Valladares, M., Zeppezauer, M., and Adolph, H.
W. (1999) Mono- and binuclear Zn2+-beta-lactamase. Role of the
conserved cysteine in the catalytic mechanism, J. Biol. Chem. 274,
13242-13249.
7. Concha, N. O., Rasmussen, B. A., Bush, K., and Herzberg, O.
(1996) Crystal structure of the wide-spectrum binuclear zinc
â-lactamase from Bacteroides fragilis, Structure 4, 823-836.
8. Paul-Soto, R., Hernadez-Valladares, M., Galleni, M., Bauer, R.,
Zeppezauer, M., Fre`re, J. M., and Adolph, H. W. (1998) Monoand
binuclear Zn-beta-lactamase from Bacteroides fragilis: catalytic
and structural roles of the zinc ions, FEBS Lett. 438, 137-
140; Yang, Y., Keeney, D., Tang, X., Canfield, N., and Rasmussen,
B. A. (1999) Kinetic properties and metal content of the
metallo-â-lactamase CcrA harboring selective amino acid substitutions,
J. Biol. Chem. 274, 15706-15711.
9. Wang, Z., Fast, W., and Benkovic, S. J. (1999) On the mechanism
of the Bacteroides fragilis metallo-â-lactamase, Biochemistry 38,
10013-10023.
10. Laraki, N., Franceschini, N., Rossolini, G. M., Santucci, P.,
Meunier, C., de Pauw, E., Amicosante, G., Fre`re, J. M., and
Galleni, M. (1999) Biochemical characterisation of the Pseudomonas
aeruginosa 101/1477 metallo-â-lactamase IMP-1 produced
by Escherichia coli, Antimicrob. Agents Chemother. 43, 902-
906; Haruta, S., Yamaguchi, H., Yamamoto, E. T., Eriguchi, Y.,
Nukaga, M., O’Hara, K., and Sawai, T. (2000) Functional analysis
of the active site of a metallo-â-lactamase proliferating in Japan,
Antimicrob. Agents Chemother. 44, 2304-2309.
11. Concha, N. O., Janson, C. A., Rowling, P., Pearson, S., Cheever,
C. A., Clarke, B. P., Lewis, C., Galleni, M., Fre`re, J. M., Payne,
D. J., Bateson, J. H., and Abdel-Meguid, S. S. (2000) Crystal
structure of the IMP-1 metallo â-lactamase from Pseudomonas
aeruginosa and its complex with a mercaptocarboxylate inhibi-tor: binding determinants of a potent, broad-spectrum inhibitor,
Biochemistry 39, 4288-4298.
12. Hernandez Valladares, M., Felici, A., Weber, G., Adolph, H. W.,
Zeppezauer, M., Rossolini, G. M., Amicosante, G., Fre`re, J. M.,
and Galleni, M. (1997) Zn(II) dependence of the Aeromonas
hydrophila AE036 metallo-â-lactamase activity and stability,
Biochemistry 36, 11534-11541.
13. Crowder, M. W., Walsh, T. R., Banovic, L., Pettit, M., and
Spencer, J. (1998) Overexpression, purification, and characterization
of the cloned metallo-â-lactamase (L1) from Stenotrophomonas
maltophilia, Antimicrob. Agents Chemother. 42, 921-926.
14. Mercuri, P. S., Bouillenne, F., Boschi, L., Lamotte-Brasseur, J.,
Amicosante, G., Devreese, B., van Beeumen, J., Fre`re, J. M.,
Rossolini, G. M., and Galleni, M. (2001) Biochemical characterization
of the FEZ-1 metallo-â-lactamase of Legionella gormanii
ATCC 33297T produced in Escherichia coli, Antimicrob. Agents
Chemother. 45, 1254-1262.
15. Carfi, A., Duee, E., Galleni, M., Fre`re, J. M., and Dideberg, O.
(1998) 1.85 Å resolution structure of the zinc(II) â-lactamase from
Bacillus cereus, Acta Crystallogr., Sect. D: Biol. Crystallogr. 54,
313-323.
16. Carfi, A., Duee, E., Paul-Soto, R., Galleni, M., Fre`re, J. M., and
Dideberg, O. (1998) X-ray structure of the ZnII â-lactamase from
Bacteroides fragilis in an orthorhombic crystal form, Acta
Crystallogr., Sect. D: Biol. Crystallogr. 54, 45-57.
17. Ullah, J. H., Walsh, T. R., Taylor, I. A., Emery, D. C., Verma, C.
S., Gamblin, S. J., and Spencer, J. (1998) The crystal structure of
the L1 metallo-â-lactamase from Stenotrophomonas maltophilia
at 1.7 Å resolution, J. Mol. Biol. 284, 125-136.
18. Garcı´a-Sa´ez, P., Mercuri, S., Papamicael, C., Kahn, R., Fre`re, J.
M., Galleni, M., Rossolini, G. M., and Dideberg, O. (2003) Threedimensional
structure of FEZ-1, a monomeric subclass B3 metallo-
â-lactamase from Fluoribacter gormanii, in native form and in
complex with D-captopril, J. Mol. Biol. 325, 651-660.
19. Garau, G., Bebrone, C., Anne, C., Galleni, M., Frere, J.-M., and
Dideberg, O. (2005) A metallo-â-lactamase in action: crystal
structure of the monozinc carbapenemase CphA and its complex
with biapenem, J. Mol. Biol. 345, 785-795.
20. Garcia-Saez, I., Hopkins, J., Papamicael, C., Franceschini, N.,
Amicosante, G., Rossolini, G. M., Galleni, M., Fre`re, J. M., and
Dideberg, O. (2003) The 1.5-Å Structure of Chryseobacterium
meningosepticum zinc â-lactamase in complex with the inhibitor,
D-Captopril, J. Biol. Chem. 278, 23868-23873.
21. Fitzgerald, P. M., Wu, J. K., and Toney, J. H. (1998) Unanticipated
inhibition of the metallo-â-lactamase from Bacteroides fragilis
by 4-morpholineethanesulfonic acid (MES): a crystallographic
study at 1.85-Å resolution, Biochemistry 37, 6791-6800; Concha,
N. O., Rasmussen, B. A., Bush, K., and Herzberg, O. (1997)
Crystal structure of the cadmium- and mercury-substituted metallobeta-
lactamase from Bacteroides fragilis, Protein Sci. 6, 2671-
2676; Toney, J. H., Fitzgerald, P. M., Grover-Sharma, N., Olson,
S. H., May, W. J., Sundelof, J. G., Vanderwall, D. E., Cleary, K.
A., Grant, S. K., Wu, J. K., Kozarich, J. W., Pompliano, D. L.,
and Hammond, G. G. (1998) Antibiotic sensitization using
biphenyl tetrazoles as potent inhibitors of Bacteroides fragilis
metallo-â-lactamase, Chem. Biol. 5, 185-196.
22. Carfi, A., Pares, S., Duee, E., Galleni, M., Duez, C., Fre`re, J. M.,
and Dideberg, O. (1995) The 3-D structure of a zinc metallo-â-
lactamase from Bacillus cereus reveals a new type of protein fold,
EMBO J. 14, 4914-4921.
23. Paul-Soto, R., Zeppezauer, M., Adolph, H. W., Galleni, M., Fre`re,
J. M., Carfi, A., Dideberg, O., Wouter, J., Hemmingsen, L., and
Bauer, R. (1999) Preference of Cd(II) and Zn(II) for the two metal
sites in Bacillus cereus â-lactamase II: a perturbed angular
correlation of ç-rays (PAC) spectroscopy study, Biochemistry 38,
16500-16506.
24. Toney, J. H., Hammond, G. G., Fitzgerald, P. M., Sharma, N.,
Balkovec, J. M., Rouen, G. P., Olson, S. H., Hammond, M. L.,
Greenlee, M. L., and Gao, Y. D. (2001) Succinic acids as potent
inhibitors of plasmid-borne IMP-1 metallo-â-lactamase, J. Biol.
Chem. 276, 31913-31918.
25. Prosperi-Meys, C., Wouters, J., Galleni, M., and Lamotte-Brasseur,
J. (2001) Substrate binding and catalytic mechanism of class B
â-lactamases: a molecular modelling study, Cell. Mol. Life Sci.
58, 2136-2143.
26. Hemmingsen, L., Damblon, C., Antony, J., Jensen, M., Adolph,
H. W., Wommer, S., Roberts, G. C. K., and Bauer, R. (2001)
Dynamics of mononuclear cadmium â-lactamase revealed by the
combination of NMR and PAC spectroscopy, J. Am. Chem. Soc.
123, 10329-10335; Damblon, C., Prosperi, C., Lian, L. Y.,
Barsukov, I., Paul-Soto, R., Galleni, M., Fre`re, J. M., and Roberts,
G. C. K. (1999) 1H-15N HMQC for the identification of metalbound
histidines in 113Cd-substituted Bacillus cereus zinc â-lactamase,
J. Am. Chem. Soc. 121, 11575-11576.
27. Walter, M. W., Felici, A., Galleni, M., Paul-Soto, R., Adlington,
R. M., Baldwin, J. E., Fre`re, J. M., Golobov, M., and Schofield,
C. J. (1996) Trifluoromethyl alcohol and ketone inhibitors
of metallo-â-lactamases, Bioorg. Med. Chem. Lett. 6, 2455-
2458.
28. Walter, M. W., Hernandez-Valladares, M., Adlington, R. M.,
Amicosante, G., Baldwin, J. E., Fre`re, J. M., Galleni, M.,
Rossolini, G. M., and Schofield, C. J. (1999) Hydroxamate
inhibitors of Aeromonas hydrophila AE036 metallo-â-lactamase,
Bioorg. Chem. 27, 35-40.
29. Arawaka, Y., Shibata, N., Shibayama, K., Kurokawa, H., Yagi,
T., Fujiwara, H., and Goto, M. (2000) Convenient test for
screening metallo-â-lactamase-producing gram-negative bacteria
by using thiol compounds, J. Clin. Microbiol. 38, 40-43.
30. Bounaga, S., Laws, A. P., Galleni, M., and Page, M. I. (1998)
The mechanism of catalysis and the inhibition of the Bacillus
cereus zinc-dependent â-lactamase, Biochem J. 331, 703-711.
31. Goto, M., Takahashi, T., Yamashita, F., Koreeda, A., Mori, H.,
Ohta, M., and Arakawa, Y. (1997) Inhibition of the metallo-â-
lactamase produced from Serratia marcescens by thiol compounds,
Biol. Pharm. Bull. 20, 1136-1140.
32. Greenlee, M. L., Laub, J. B., Balkovec, J. M., Hammond, M. L.,
Hammond, G. G., Pompliano, D. L., and Epstein-Toney, J. H.
(1999) Synthesis and SAR of thioester and thiol inhibitors of
IMP-1 metallo-â-lactamase, Bioorg. Med. Chem. Lett. 9, 2549-
2554.
33. Mollard, C., Moali, C., Papamicael, C., Damblon, C., Vessilier,
S., Amicosante, G., Schofield, C. J., Galleni, M., Fre`re, J. M.,
and Roberts, G. C. K. (2001) Thiomandelic acid, a broad-spectrum
inhibitor of zinc â-lactamases: kinetic and spectroscopic studies,
Biol. Chem. 276, 45015-45023.
34. Bounaga, S., Galleni, M., Laws, A. P., and Page, M. I (2001)
Cysteinyl peptide inhibitors of Bacillus cereus zinc beta-lactamase,
Bioorg. Med. Chem. 9, 503-510.
35. Hammond, G. G., Huber, J. L., Greenlee, M. L., Laub, J. B.,
Young, K., Silver, L. L., Balkovec, J. M., Pryor, K. D., Wu, J.
K., Leiting, B., Pompliano, D. L., and Toney, J. H. (1999)
Inhibition of IMP-1 metallo-â-lactamase and sensitisation of IMP-
1-producing bacteria by thioester derivatives, FEMS Microbiol.
Lett. 179, 289-296.
36. Payne, D. J., Bateson, J. H., Gasson, B. C., Proctor, D., Khushi,
T., Farmer, T. H., Toldon, D. A., Bell, D., Skett, P. W., Marshall,
A. C., Reid, R., Ghosez, L., Combret, Y., and Marchand-Brynaert,
J. (1997) Inhibition of metallo-â-lactamases by a series of
mercaptoacetic acid thiol ester derivatives, Antimicrob. Agents
Chemother. 41, 135-140; Payne, D. J., Bateson, J. H., Gasson,
B. C., Khushi, T., Proctor, D., Pearson, S. C., and Reid, R. (1997)
Inhibition of metallo-â-lactamases by a series of thiol ester
derivatives of mercapto-phenylacetic acid, FEMS Microbiol. Lett.
157, 171-175.
37. Toney, J. H., Fitzgerald, P. M., Grover-Sharma, N., Olson, S. H.,
May, W. J., Sundelof, J. G., Vanderwall, D. E., Cleary, K. A.,
Grant, S. K., Wu, J. K., Kozarich, J. W., Pompliano, D. L., and
Hammond, G. G. (1998) Antibiotic sensitization using biphenyl
tetrazoles as potent inhibitors of Bacteroides fragilis metallo-â-
lactamase, Chem. Biol. 5, 185-196; Toney, J. H., Cleary, K. A.,
Hammond, G. G., Yuan, X., May, W. J., Hutchins, S. M., Ashton,
W. T., and Vanderwall, D. E. (1999) Structure-activity relationships
of biphenyl tetrazoles as metallo-â-lactamase inhibitors,
Bioorg. Med. Chem. Lett. 9, 2741-2746.
38. Payne, D. J., Hueso-Rodrı´guez, J. A., Boyd, H., Concha, N. O.,
Janson, C. A., Gilpin, M., Bateson, J. H., Cheever, C., Niconovich,
N. L., Pearson, S., Rittenhouse, S., Tew, D., Dı´ez, E., Pe´rez, P.,
De La Fuente, J., Rees, M., and Rivera-Sagredo, A. (2002)
Identification of a series of tricyclic natural products as potent
broad-spectrum inhibitors of metallo-â-lactamases, Antimicrob.
Agents Chemother. 46, 1880-1886.
39. Siemann, S., Evanoff, D. P., Marrone, L., Clarke, A. J., Viswantha,
T., and Dimitrenko, G. I. (2002) N-arylsulfonyl hydrazones as
inhibitors of IMP-1 metallo-â-lactamase, Antimicrob. Agents
Chemother. 46, 2450-2457.
40. Wang, Z., and Benkovic, S. J. (1998) Purification, characterization,
and kinetic studies of a soluble Bacteroides fragilis metallo-â-lactamase that provides multiple antibiotic resistance, J. Biol.
Chem. 273, 22402-22408.
41. Davies, A., M., and Page, M. I. (1985) Opening of the thiazolidine
ring of penicillin derivatives, J. Chem. Soc., Chem. Commun.,
1702-1704.
42. Pratt, R. F., and Faraci, W. S. (1986) Direct observation by 1H
NMR of cephalosporoate intermediates in aqueous solution during
the hydrazinolysis and â-lactamase-catalyzed hydrolysis of cephalosporins
with 3¢ leaving groups: kinetics and equilibria of the 3¢
elimination reaction, J. Am. Chem. Soc. 108, 5328-5333; Bundgaard,
H. (1977) Isolation and characterization of cephalexin
degradation products formed in neutral aqueous solution, Arch.
Pharm. Chemi, Sci. Ed. 5, 149-155. Vilanova, B., Frau, J.,
Donoso, J., Munoz, F., and Garcia Blanco, F. G. (1997) â-Lactamase-
catalysed hydrolysis of cephalexin: evolution of the
cephalosporoate intermediate, J. Chem. Soc., Perkin Trans. 2,
2439-2444.
43. Morrison, J. F., and Walsh, C., T. (1988) The behavior and
significance of slow-binding enzyme inhibitors, AdV. Enzymol.
Relat. Areas Mol. Biol. 61, 201-301.
44. Ellman, G. L. (1959) Tissue sulfhydryl groups, Arch. Biochem.
Biophys. 82, 70-77; Riddles, P. W., Blakeley, R. L., and Zerner,
B. (1979) Ellman’s reagent: 5,5¢-dithiobis(2-nitrobenzoic acid)s
a reexamination, Anal. Biochem. 94, 75-81.
45. Bundgaard, H. (1976) Hydrolysis and intramolecular aminolysis
of cephalexin and cephaloglycin in aqueous solution, Arch. Pharm.
Chemi, Sci. Ed. 4, 25-43.
46. Dinner, A. (1977) Cephalosporin degradations, J. Med. Chem. 20,
963-965.
47. Vilanova, B., Munoz, F., Donoso, J., and Garcia Blanco, F. (1993)
Degradation of cephaloridine on alkaline hydrolysis, HelV. Chim.
Acta 76, 1619-1625.
48. Page, M. I. (1987) The mechanisms of reactions of â-lactam
antibiotics, AdV. Phys. Org. Chem. 23, 165-270.
49. Pelton, J. G., Torchia, D. A., Meadow, N. D., and Roseman, S.
(1993) Tautomeric states of the active-site histidines of phosphorylated
and unphosphorylated III(Glc), a signal-transducing protein
from Escherichia coli, using two-dimensional heteronuclear NMR
techniques, Protein Sci. 2, 543-558.
50. Damblon, C., Jensen, M., Ababou, A., Barsukov, I., Papamicael,
C., Schofield, C. J., Olsen, L., Bauer, R., and Roberts, G. C. (2003)
The inhibitor thiomandelic acid binds to both metal ions in
metallo-beta-lactamase and induces positive cooperativity in metal
binding, J. Biol. Chem. 278, 29240-29251.
51. Siemann, S., Clarke, A. J., Viswanatha, T., and Dmitrienko, G. I.
(2003) Thiols as classical and slow-binding inhibitors of IMP-1
and other binuclear metallo-â-lactamases, Biochemistry 42, 1673-
1683.
52. Ghebre-Sellassie, I., Hem, S. L., and Knevel, A. M. (1984)
Epimerization of benzylpenicilloic acid in alkaline media, J.
Pharm. Sci. 73, 125-128.
BI050302J |
|---|
Tools
Tools