Home LiteratureArticle Details
PMID: 7695305 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Kinetic analysis of extension of substrate specificity with Xanthomonas maltophilia, Aeromonas hydrophila, and Bacillus cereus metallo-beta-lactamases.

Antimicrobial agents and chemotherapy ·Vol. 39 ·No. 1 ·1995-01-00 ·Pages 192-9

Felici A, Amicosante G

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
  1. 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
  2. Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia.
    Biochim Biophys Acta. 1994 Jun 21;1218(2):199-201 PMID: 8018721
  3. 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
  4. 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
  5. The structure of beta-lactamases.
    Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321-31 PMID: 6109327
  6. 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
  7. Automated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.
    Biochem Pharmacol. 1987 Jul 15;36(14):2393-403 PMID: 3038122
  8. 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
  9. 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
  10. 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
  11. Serine beta-lactamases and penicillin-binding proteins.
    Annu Rev Microbiol. 1991;45:37-67 PMID: 1741619
  12. An overview of the kinetic parameters of class B beta-lactamases.
    Biochem J. 1993 Apr 1;291 ( Pt 1):151-5 PMID: 8471035
  13. 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
  14. Metallo-beta-lactamases--a new therapeutic challenge.
    J Med Microbiol. 1993 Aug;39(2):93-9 PMID: 8345513
  15. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1995-01-00
Pages
192-9
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC162508
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]