Home LiteratureArticle Details
PMID: 242252 Published · ppublish English Journal Article

Production and property of beta-lactamases in Streptomyces.

Antimicrobial agents and chemotherapy ·Vol. 8 ·No. 4 ·1975-10-00 ·Pages 402-8

Ogawara H

Abstract

The production of beta-lactamases by 100 strains of Streptomyces was studied. About one-half of the strains produced more than 2.3 U of beta-lactamase per ml, and another half produced less than 1.4 U/ml. The amounts of beta-lactamases produced by two strains were in the order of those produced by Bacillus cereus 569/H and Bacillus licheniformis 749/C. These Streptomyces enzymes function primarily as penicillinases rather than cephalosporinases. Properties such as pH optimum, substrate specificity, and heat stability suggest that these Streptomyces beta-lactamases are closely related to each other. In contrast to bacterial beta-lactamases, Streptomyces beta-lactamases were insusceptible to inactivation by N-bromosuccinimide and only slightly susceptible to iodine. This suggests that the construction mode of the active site would be different from other beta-lactamases. Studies on the minimum inhibitory concentrations of benzylpenicillin to seven Streptomyces strains and on their maximum beta-lactamase production indicate that the susceptibility of Streptomyces to penicillin is not directly related to the beta-lactamase production.

MeSH Terms
Amidohydrolases/biosynthesis Cephalosporinase/biosynthesis,metabolism Culture Media Drug Stability Hydrogen-Ion Concentration Microbial Sensitivity Tests Penicillin G/pharmacology Penicillinase/biosynthesis,metabolism Streptomyces/enzymology Time Factors beta-Lactamase Inhibitors
Chemicals
Culture Media beta-Lactamase Inhibitors Amidohydrolases Cephalosporinase Penicillinase Penicillin G
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Ogawara H
References (6)
6 references, click to expand
  1. Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells.
    Ann N Y Acad Sci. 1974 May 10;235(0):210-24 PMID: 4277601
  2. The biochemistry and function of beta-lactamase (penicillinase).
    Adv Enzymol Relat Areas Mol Biol. 1966;28:237-323 PMID: 5334062
  3. The function and evolution of penicillinase.
    Proc R Soc Lond B Biol Sci. 1971 Dec 31;179(1057):385-401 PMID: 4401417
  4. Exocellular beta-lactamases of Streptomyces albus G and strains R39 and K11.
    Antimicrob Agents Chemother. 1973 Feb;3(2):289-98 PMID: 4494518
  5. An introspective view of penicillinase.
    J Cell Physiol. 1970 Dec;76(3):397-403 PMID: 4993702
  6. Isolation of covalently closed circular deoxyribonucleic acid from Streptomyces coelicolor A3(2).
    J Bacteriol. 1975 Feb;121(2):416-21 PMID: 1112770
Article Info
Journal
Antimicrobial agents and chemotherapy
Abbr.
Antimicrob Agents Chemother
ISSN
0066-4804
Published
1975-10-00
Pages
402-8
Language
English
Region
United States
NLM ID
0315061
PMCID
PMC429356
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]