Abstract
Twenty beta-lactam molecules, including penicillins, cephalosporins, penems, carbapenems, and monobactams, were investigated as potential substrates for Xanthomonas maltophilia ULA-511, Aeromonas hydrophila AE036, and Bacillus cereus 5/B/6 metallo-beta-lactamases. A detailed analysis of the kinetic parameters examined confirmed these enzymes to be broad-spectrum beta-lactamases with different ranges of catalytic efficiency. Cefoxitin and moxalactam, substrates for the beta-lactamases from X. maltophilia ULA-511 and B. cereus 5/B/6, behaved as inactivators of the A. hydrophila AE036 metallo-beta-lactamase, which appeared to be unique among the enzymes tested in this study. In addition, we report a new, faster, and reliable purification procedure for the B. cereus 5/B/6 metallo-beta-lactamase, cloned in Escherichia coli HB101.
MeSH Terms
Aeromonas hydrophila/drug effects
Anti-Bacterial Agents/chemistry,pharmacology
Bacillus cereus/drug effects
Kinetics
Molecular Structure
Substrate Specificity
Xanthomonas/drug effects
beta-Lactamase Inhibitors
beta-Lactamases/isolation & purification
beta-Lactams
Chemicals
Anti-Bacterial Agents
beta-Lactamase Inhibitors
beta-Lactams
beta-Lactamases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Felici A
Dipartimento di Scienze e Tecnologie Biomediche e di Biometria, Università degli Studi dell'Aquila, Italy.
Amicosante G
References (15)
15 references, click to expand
-
Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains.
J Bacteriol. 1970 Jan;101(1):218-31
PMID: 4983650
-
Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201
PMID: 8018721
-
Separation, purification and properties of beta-lactamase I and beta-lactamase II from Bacillus cereus 569/H/9.
Biochem J. 1974 Oct;143(1):115-27
PMID: 4219278
-
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
Anal Biochem. 1976 May 7;72:248-54
PMID: 942051
-
The structure of beta-lactamases.
Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321-31
PMID: 6109327
-
Interaction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39.
Biochem J. 1982 Dec 1;207(3):437-44
PMID: 6299270
-
Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.
Biochem Pharmacol. 1987 Jul 15;36(14):2393-403
PMID: 3038122
-
Cloning, nucleotide sequence, and expression of the Bacillus cereus 5/B/6 beta-lactamase II structural gene.
J Bacteriol. 1988 Jun;170(6):2873-8
PMID: 3131315
-
Cloning and sequencing of the class B beta-lactamase gene (ccrA) from Bacteroides fragilis TAL3636.
Antimicrob Agents Chemother. 1990 Aug;34(8):1590-2
PMID: 2121094
-
Site-directed mutagenesis of dicarboxylic acids near the active site of Bacillus cereus 5/B/6 beta-lactamase II.
Biochem J. 1991 Jun 1;276 ( Pt 2):401-4
PMID: 1904717
-
Serine beta-lactamases and penicillin-binding proteins.
Annu Rev Microbiol. 1991;45:37-67
PMID: 1741619
-
An overview of the kinetic parameters of class B beta-lactamases.
Biochem J. 1993 Apr 1;291 ( Pt 1):151-5
PMID: 8471035
-
A class-A beta-lactamase from Pseudomonas stutzeri that is highly active against monobactams and cefotaxime.
Biochem J. 1993 Jun 15;292 ( Pt 3):697-700
PMID: 8318000
-
Metallo-beta-lactamases--a new therapeutic challenge.
J Med Microbiol. 1993 Aug;39(2):93-9
PMID: 8345513
-
Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
Nature. 1970 Aug 15;227(5259):680-5
PMID: 5432063