Cefcapene inactivates chromosome-encoded class C β-lactamases

Journal of Infection and Chemotherapy

Volumn 8, Issue 3, 2002, Pages 207-210

  Alba, Jimena ^a,b   Ishii, Yoshikazu ^b,c   Galleni, Moreno ^c   Frère, Jean Marie ^c   Ito, Masahiko ^a   Yamaguchi, Keizo ^b  

^a UNIVERSITY OF YAMANASHI   (Japan)

^b TOHO UNIVERSITY   (Japan)

^c UNIVERSITY OF LIÈGE   (Belgium)

Author keywords

Cefcapene; Inactivation of class C lactamase; Lactamase

Indexed keywords

BETA LACTAMASE; CEFCAPENE; CEFPODOXIME;

ACYLATION; ANTIBACTERIAL ACTIVITY; ARTICLE; CHROMOSOME INACTIVATION; DRUG EFFECT; DRUG STABILITY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME SUBSTRATE; HYDROLYSIS; STEADY STATE;

EID: 0036746698     PISSN: 1341321X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10156-002-0177-7     Document Type: Article

References (26)

1. Ambler RP. The structure of β-lactamases. Philos Trans R Soc Lond (Biol) 1980;289:321-31.
2. Bush K, Jacoby GA, Medeiros AA. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother 1995;39:1211-33.
3. Galleni M, Lamotte-Brasseur J, Rossolini GM, Spencer J, Dideberg O, Frère JM. Standard numbering scheme for class B β-lactamases. Antimicrob Agents Chemother 2001;5:660-3.
4. Osano E, Arakawa Y, Wacharotayankun R, Ohta M, Horii T, Ito H, et al. Molecular characterization of an enterobacterial metallo β-lactamase found in a clinical isolate of Serraria marcescens that shows imipenem resistance. Antimicrob Agents Chemother 1994;87:71-8.
5. Gonzalez Leiza M, Perez-Diaz JC, Ayala J, Casellas JM, Martinez-Beltran J, Bush K, Baquero F. Gene sequence and biochemical characterization of FOX-1 from Klebsiella pneumoniae, a new AmpC-type plasmid-mediated β-lactamase with two molecular variants. Antimicrob Agents Chemother 1994;38:2150-7.
6. LAT-1) found in Klebsiella pneumoniae. Antimicrob Agents Chemother 1994;38:2207-9.
7. CMY-1 gene and its relationship with other β-lactamase genes. Antimicrob Agents Chemother 1996;40:1926-30.
8. Therrien C, Levesque RC. Molecular basis of antibiotic resistance and β-lactamase inhibition by mechanism-based inactivators: perspectives and future directions. FEMS Microbiol Rev 2000;24:251-62.
9. Yang Y, Janota K, Tabei K, Huang N, Siegel MM, Lin YI, et al. Mechanism of inhibition of the class A β-lactamases PC1 and TEM-1 by tazobactam. Observation of reaction products by electrospray ionization mass spectrometry. J Biol Chem 2000;275: 26674-82.
10. Toney JH, Hammond GG, Fitzgerald PM, Sharma N, Balkovec JM, Rouen GP, et al. Succinic acids as potent inhibitors of plasmidborne IMP-1 metallo-β-lactamase. J Biol Chem 2001;276:31913-8.
11. Concha NO, Janson CA, Rowling P, Pearson S, Cheever CA, Clarke BP, et al. 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. Biochemistry 2000;39:4288-98.
12. Crichlow GV, Nukaga M, Doppalapudi VR, Buynak JD, Knox JR. Inhibition of class C β-lactamases: structure of a reaction intermediate with a cephem sulfone. Biochemistry 2001;40:6233-9.
13. Pratt RF, Hammar NJ. Salicyloyl cyclic phosphate, a "penicillin-like" inhibitor of β-lactamases. J Am Chem Soc 1998;120:3004-6.
14. Sandanayaka VP, Yang Y. Dipolar cycloaddition of novel 6- (nitrileoxidomethyl) penam sulfone: an efficient route to a new class of β-lactamase inhibitors. Org Lett 2000;2:3087-90.
15. Patera A, Blaszczak LC, Shoichet BK. Crystal structures of substrate and inhibitor complexes with AmpC β-lactamase: possible implications for substrate-assisted catalysis. J Am Chem Soc 2000;122:10504-12.
16. Hubschwerlen C, Angehrn P, Gubernator K, Page MG, Specklin JL. Structure-based design of β-lactamase inhibitors. 2. Synthesis and evaluation of bridged sulfactams and oxamazins. J Med Chem 1998;41:3972-5.
17. Curley K, Pratt RF. Effectiveness of tetrahedral adducts as transition-state analogs and inhibitors of the class C β-lactamase of Enterobacter cloacae P99. J Am Chem Soc 1997;119:1529-38.
18. Neuwirth C, Labia R, Siebor E, Pechinot A, Madec S, Chaibi EB, Kazmierczak A. Characterization of TEM-56, a novel β-lactamase produced by a Klebsiella pneumoniae clinical isolate. Antimicrob Agents Chemother 2000;44:453-5.
19. Bouillenne F, Matagne A, Joris B, Frère JM. Technique for a rapid and efficient purification of the SHV-1 and PSE-2 β-lactamases. J Chromatogr B Biomed Sci Appl 2000;737:261-5.
20. Ishii Y, Ohno A, Taguchi H, Imajo S, Ishiguro M, Matsuzawa H. Cloning and sequence of the gene encoding a cefotaximehydrolyzing class A β-lactamase isolated from Escherichia coli. Antimicrob Agents Chemother 1995;39:2269-75.
21. Mariotte-Boyer S, Nicolas-Chanoine MH, Labia R. A kinetic study of NMC-A β-lactamase, an Ambler class A carbapenemase also hydrolyzing cephamycins. FEMS Microb Lett 1996;143:29-33.
22. Walsh TR, Hall L, Assinder SJ, Nichols WW, Cartwright SJ, MacGowan AP, Bennett PM. Sequence analysis of the L1 metalloβ-lactamase from Xanthomonas maltophilia. Biochim Biophys Acta 1994;1218:199-201.
23. Rasmussen BA, Gluzman Y, Tally FP. Escherichia coli chromosomal mutations that permit direct cloning of the Bacteroides fragilis metallo-β-lactamase gene. ccrA. Mol Microbiol 1991;5:1211-9.
24. De Meester F, Joris B, Reckinger G, Bellefroid-Bourguignon C, Frère JM, Waley SG. Automated analysis of enzyme inactivation phenomena. Application to β-lactamases and DD-peptidases. Biochem Pharmacol 1987;36:2393-403.
25. Galleni M, Frère JM. A survey of the kinetic parameters of class C β-lactamases. Penicillins Biochem J 1988;255:119-22.
26. Dubus A, Wilkin JM, Raquet X, Normark S, Frère JM. Catalytic mechanism of active-site serine β-lactamases: role of the conserved hydroxy group of the Lys-Thr (Ser)-Gly triad. Biochem J 1994;301:485-94.