[en] A gene (bla) encoding a beta-lactamase is present in the cephamycin gene cluster of Streptomyces clavuligerus, the strain producing clavulanic acid and a beta-lactamase inhibitory protein. The bla gene is located 5.1 kb downstream from and in the opposite orientation to cefE, encoding the deacetoxycephalosporin C synthase. The bla gene encodes a 332-residue protein (Mr, 35,218), similar to other class A beta-lactamases produced by actinomycetes. Modification (to SDG) of the SDN conserved motif of class A beta-lactamases as well as of amino acids in otherwise conserved regions in the molecule may explain the low penicillinase and cephalosporinase activities of the protein. The beta-lactamase has been purified to homogeneity and found to bind [3H]benzylpenicillin, a result reflecting a rate-limiting deacylation step. Nucleotide sequences homologous to bla were found in all tested cephamycin producers, but several other Streptomyces species which produce a beta-lactamase do not contain genes for beta-lactam antibiotic biosynthesis.
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Bibliography
Aharonowitz, Y., G. Cohen, and J. F. Martín. 1992. Penicillin and cephalosporin biosynthetic genes: structure, organization, regulation and evolution. Annu. Rev. Microbiol. 46:461-495.
Ambler, R. P., A. F. Coulson, J. M. Frère, J. M. Ghuysen, B. Jaurin, B. Joris, R. Levesque, G. Tiraby, and S. G. Waley. 1991. The structure of β-lactamases. Biochem. J. 276:269-272.
Benveniste, R., and J. Davies. 1973. Aminoglycoside antibiotic-inactivating enzymes in actinomycetes similar to those present in clinical isolates of antibiotic-resistant bacteria. Proc. Natl. Acad. Sci. USA 70:2276-2280.
Brown, A. G., D. Butterworth, M. Cole, G. Hanscomb, J. D. Hood, and C. Reading. 1976. Naturally occurring β-lactamase inhibitors with antibacterial activity. J. Antibiot. 29:668-669.
Coque, J. J. R., P. Liras, and J. F. Martín. 1993. Genes for a β-lactamase, a penicillin-binding protein and a transmembrane protein are clustered with the cephamycin biosynthetic genes in Nocardia lactamdurans. EMBO J. 12:631-639.
Coutoure, F., J. Lachapelle, and R. C. Levesque. 1992. Phylogeny of LCR-1 and Oxa-5 with class A and class D β-lactamases. Mol. Microbiol. 6:1693-1705.
Cundliffe, E. 1989. How antibiotic-producing organisms avoid suicide. Annu. Rev. Microbiol. 43:207-223.
Doran, J. L., B. K. Leskiw, S. Aippersbach, and S. E. Jensen. 1990. Isolation and characterization of a β-lactamase-inhibitory protein from Streptomyces clavuligerus and cloning and analysis of the corresponding gene. J. Bacteriol. 172:4909-4918.
Forsman, M., B. Haggstrom, L. Lindgren, and B. Jaurin. 1990. Molecular analysis of β-lactamases from four species of Streptomyces: comparison of amino acid sequences with those of other β-lactamases. J. Gen. Microbiol. 136:589-598.
Frère, J. M. 1995. β-Lactamases and bacterial resistance to antibiotics. Mol. Microbiol. 16:385-395.
Hall, A., and J. R. Knowles. 1976. Directed selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme function. Nature 264:803-804.
Herzberg, O., G. Kapadia, B. Blanco, T. S. Smith, and A. Coulson. 1991. Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1. Biochemistry 30:9503-9509.
Hopwood, D. A., M. J. Bibb, K. F. Chater, T. Kieser, C. J. Bruton, H. M. Kieser, D. J. Lydiate, C. P. Smith, J. M. Ward, and H. Schrempf. 1985. Genetic manipulation of Streptomyces: a laboratory manual. The John Innes Foundation, Norwich, England.
Jacob, F., B. Joris, S. Lepage, J. Dusart, and J. M. Frère. 1990. Role of the conserved amino acids of the SDN loop (Ser130, Asp131 and Asn132) in a class A β-lactamase studied by site-directed mutagenesis. Biochem. J. 271:399-406.
Jaurin, B., M. Forsman, and B. Haggstrom. 1988. β-Lactamase genes of Streptomyces badius. Streptomyces cacaoi and Streptomyces fradiae: cloning and expression in Streptomyces lividans. Biochim. Biophys. Acta 949:288-296.
Joris, B., P. Ledent, O. Dideberg, E. Fonzé, J. Lamotte-Brasseur, J. A. Kelly, J. M. Ghuysen, and J. M. Frère. 1991. Comparison of the sequences of class A β-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Antimicrob. Agents Chemother. 35:2294-2301.
Kimura, H., H. Miyashita, and Y. Sumino. 1996. Organization and expression in Pseudomonas putida of the gene cluster involved in cephalosporin biosynthesis from Lysobacter lactamgenus YK90. Appl. Microbiol. Biotechnol. 45:490-501.
Kovacevic, S., M. B. Tobin, and J. R. Miller. 1990. The β-lactam biosynthesis genes for isopenicillin N epimerase and deacetoxycephalosporin C synthetase are expressed from a single transcript in Streptomyces clavuligerus. J. Bacteriol. 172:3952-3958.
Kumar, C. V., J. L. de la Fuente, A. L. Leitão, P. Liras, and J. F. Martín. 1996. Effect of amplification or targeted disruption of the β-lactamase gene of Nocardia lactamdurans on cephamycin biosynthesis. Appl. Microbiol. Biotechnol. 45:621-628.
Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
Lamotte-Brasseur, J., G. Dive, O. Dideberg, P. Charlier, J. M. Frère, and J. M. Ghuysen. 1991. Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G. Biochem. J. 279:213-221.
Matagne, A., B. Joris, J. Van Beeumen, and J. M. Frère. 1991. Ragged N-termini and other variants of class A β-lactamases analysed by chromato-focusing. Biochem. J. 273:503-510.
Matagne, A., A. M. Misselyn-Bauduin, B. Joris, T. Erpicum, B. Granier, and J. M. Frère. 1990. The diversity of the catalytic properties of class A β-lactamases. Biochem. J. 265:131-146.
O'Callaghan, C. H., A. Morris, S. Kirby, and A. Shingler. 1972. A novel method for detection of β-lactamases by using a chromogenic cephalosporin substrate. Antimicrob. Agents Chemother. 1:283-288.
Ogawara, H. 1975. Production and properties of beta-lactamase in Streptomyces. Antimicrob. Agents Chemother. 8:402-408.
Ogawara, H., and S. Horikawa. 1980. Penicillin-binding proteins of Streptomyces cacaoi, Streptomyces olivaceus, and Streptomyces clavuligerus. Antimicrob. Agents Chemother. 17:1-7.
Raquet, X., J. Lamotte-Brasseur, E. Fonzé, S. Goussard, P. Courvalin, and J. M. Frère. 1994. TEM β-lactamase mutants hydrolysing third-generation cephalosporins. J. Mol. Biol. 244:625-639.
Romero, J., P. Liras, and J. F. Martín. 1984. Isolation and biochemical characterization of Streptomyces davuligerus mutants in the biosynthesis of clavulanic acid and cephamycin C. Appl. Microbiol. Biotechnol. 20:318-325.
Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
Sendouda, A., H. Urabe, and H. Ogawara. 1993. Cloning, nucleotide sequence and expression of a β-lactamase gene from Streptomyces lavendulae. FEMS Microbiol. Lett. 112:343-348.
Sougakoff, W., A. Petit, S. Goussard, D. Sirot, A. Bure, and P. Courvalin. 1989. Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum β-lactamases TEM-4 and TEM-5 in Enterobacteriaceae. Gene 78:339-348.
Strynadka, N. C. J., S. Jensen, K. Johns, H. Blanchard, M. Page, A. Matagne, J. M. Frère, and M. N. G. James. 1994. Structural and kinetic characterization of a β-lactamase-inhibitor protein. Nature 368:657-660.
Takano, E., J. White, C. J. Thompson, and M. J. Bibb. 1995. Construction of thiostrepton-inducible, high copy-number expression vector for use in Streptomyces spp. Gene 166:133-137.
Ward, J. M., and J. E. Hodgson. 1993. The biosynthetic genes for clavulanic acid and cephamycin production occur as a "super-cluster" in three Streptomyces. FEMS Microbiol. Lett. 110:239-242.
Yu, H., E. Serpe, J. Romero, J. J. R. Coque, K. Maeda, M. Oelgeschläger, G. Hintermann, P. Liras, J. F. Martín, A. L. Demain, and J. Piret. 1994. Possible involvement of the lysine Σ-aminotransferasc gene (lat) in the expression of the genes encoding ACV synthetase (pcbAB) and isopenicillin N synthase (pcbC) in Streplomyces davuligerus. Microbiology 140:3367-3377.
Similar publications
Sorry the service is unavailable at the moment. Please try again later.
This website uses cookies to improve user experience. Read more
Save & Close
Accept all
Decline all
Show detailsHide details
Cookie declaration
About cookies
Strictly necessary
Performance
Strictly necessary cookies allow core website functionality such as user login and account management. The website cannot be used properly without strictly necessary cookies.
This cookie is used by Cookie-Script.com service to remember visitor cookie consent preferences. It is necessary for Cookie-Script.com cookie banner to work properly.
Performance cookies are used to see how visitors use the website, eg. analytics cookies. Those cookies cannot be used to directly identify a certain visitor.
Used to store the attribution information, the referrer initially used to visit the website
Cookies are small text files that are placed on your computer by websites that you visit. Websites use cookies to help users navigate efficiently and perform certain functions. Cookies that are required for the website to operate properly are allowed to be set without your permission. All other cookies need to be approved before they can be set in the browser.
You can change your consent to cookie usage at any time on our Privacy Policy page.
