The pH-dependence of class B and class C beta-lactamases
- PMID: 6604522
- PMCID: PMC1152090
- DOI: 10.1042/bj2130061
The pH-dependence of class B and class C beta-lactamases
Abstract
The classification by structure allots beta-lactamases to (at present) three classes, A, B and C. The pH-dependence of the kinetic parameters for class B and class C have been determined. They differ from each other and from class A beta-lactamases. The class B enzyme was beta-lactamase II from Bacillus cereus 569/H/9. The plots of kcat against pH for the hydrolysis of benzylpenicillin by Zn(II)-requiring beta-lactamase II and Co(II)-requiring beta-lactamase II were not symmetrical, but those of kcat/Km were. A similar feature was observed for the hydrolysis of both benzylpenicillin and cephalosporin C by a class C beta-lactamase from Pseudomonas aeruginosa. The results have been interpreted by a scheme in which two ionic forms of an intermediate can give product, but do so at differing rates.
Similar articles
-
A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate.Biochem J. 1989 Mar 15;258(3):765-8. doi: 10.1042/bj2580765. Biochem J. 1989. PMID: 2499308 Free PMC article.
-
The mechanism of catalysis and the inhibition of the Bacillus cereus zinc-dependent beta-lactamase.Biochem J. 1998 May 1;331 ( Pt 3)(Pt 3):703-11. doi: 10.1042/bj3310703. Biochem J. 1998. PMID: 9560295 Free PMC article.
-
Changes in the coordination geometry of the active-site metal during catalysis of benzylpenicillin hydrolysis by Bacillus cereus beta-lactamase II.Biochemistry. 1986 Nov 4;25(22):7208-15. doi: 10.1021/bi00370a066. Biochemistry. 1986. PMID: 3099831
-
Cryoenzymology of Bacillus cereus beta-lactamase II.Biochemistry. 1985 Nov 19;24(24):6876-87. doi: 10.1021/bi00345a021. Biochemistry. 1985. PMID: 3935166
-
Enzyme deactivation due to metal-ion dissociation during turnover of the cobalt-beta-lactamase catalyzed hydrolysis of beta-lactams.Biochemistry. 2006 Sep 12;45(36):11012-20. doi: 10.1021/bi0610146. Biochemistry. 2006. PMID: 16953588
Cited by
-
Substrate-promoted formation of a catalytically competent binuclear center and regulation of reactivity in a glycerophosphodiesterase from Enterobacter aerogenes.J Am Chem Soc. 2008 Oct 29;130(43):14129-38. doi: 10.1021/ja803346w. Epub 2008 Oct 3. J Am Chem Soc. 2008. PMID: 18831553 Free PMC article.
-
The diversity of the catalytic properties of class A beta-lactamases.Biochem J. 1990 Jan 1;265(1):131-46. doi: 10.1042/bj2650131. Biochem J. 1990. PMID: 2302162 Free PMC article.
-
The beta-lactamase of Enterobacter cloacae P99. Chemical properties, N-terminal sequence and interaction with 6 beta-halogenopenicillanates.Biochem J. 1985 May 15;228(1):241-8. doi: 10.1042/bj2280241. Biochem J. 1985. PMID: 2988516 Free PMC article.
-
Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia.J Biol Inorg Chem. 2006 Apr;11(3):351-8. doi: 10.1007/s00775-006-0083-z. Epub 2006 Feb 18. J Biol Inorg Chem. 2006. PMID: 16489411
-
A thiono-beta-lactam substrate for the beta-lactamase II of Bacillus cereus. Evidence for direct interaction between the essential metal ion and substrate.Biochem J. 1989 Mar 15;258(3):765-8. doi: 10.1042/bj2580765. Biochem J. 1989. PMID: 2499308 Free PMC article.
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources