Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1988 Apr 1;251(1):73–79. doi: 10.1042/bj2510073

Complete amino acid sequence of p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1).

M Barthélémy 1, J Peduzzi 1, R Labia 1
PMCID: PMC1148965  PMID: 3260490

Abstract

The complete amino acid sequence of the p453-plasmid-mediated PIT-2 beta-lactamase (SHV-1) was determined. The protein contains 265 residues. Peptides resulting from digestions with trypsin, Staphylococcus aureus V8 proteinase, chymotrypsin and Lys-C proteinase and cleavage with CNBr were separated and purified by using reverse-phase h.p.l.c. The amino acid sequence of each peptide was manually determined with the dimethylaminoazobenzene isothiocyanate/phenyl isothiocyanate double-coupling method. The primary structure of PIT-2 beta-lactamase was compared with those of two closely related enzymes, namely TEM-1 beta-lactamase and the beta-lactamase of Klebsiella pneumoniae strain LEN-1. The PIT-2 beta-lactamase amino acid sequence was strongly retained, with respectively 68% and 88% homology. Thus PIT-2 enzyme could represent an evolutionary step between a chromosomally encoded beta-lactamase and the plasmid-mediated TEM beta-lactamases.

Full text

PDF
73

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambler R. P., Brown L. H. The amino acid sequence of Pseudomonas fluorescens azurin. Biochem J. 1967 Sep;104(3):784–825. doi: 10.1042/bj1040784. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ambler R. P., Scott G. K. Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3732–3736. doi: 10.1073/pnas.75.8.3732. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Ambler R. P. The structure of beta-lactamases. Philos Trans R Soc Lond B Biol Sci. 1980 May 16;289(1036):321–331. doi: 10.1098/rstb.1980.0049. [DOI] [PubMed] [Google Scholar]
  4. Arakawa Y., Ohta M., Kido N., Fujii Y., Komatsu T., Kato N. Close evolutionary relationship between the chromosomally encoded beta-lactamase gene of Klebsiella pneumoniae and the TEM beta-lactamase gene mediated by R plasmids. FEBS Lett. 1986 Oct 20;207(1):69–74. doi: 10.1016/0014-5793(86)80014-x. [DOI] [PubMed] [Google Scholar]
  5. Barthélémy M., Peduzzi J., Labia R. Distinction entre les structures primaires des beta-lactamases TEM-1 et TEM-2. Ann Inst Pasteur Microbiol. 1985 May-Jun;136A(3):311–321. doi: 10.1016/s0769-2609(85)80093-4. [DOI] [PubMed] [Google Scholar]
  6. Barthélémy M., Peduzzi J., Labia R. N-terminal amino acid sequence of PIT-2 beta-lactamase (SHV-1) J Antimicrob Chemother. 1987 Jun;19(6):839–841. doi: 10.1093/jac/19.6.839. [DOI] [PubMed] [Google Scholar]
  7. Barthélémy M., Peduzzi J., Verchère-Beaur C., Ben Yaghlane H., Labia R. Purification and biochemical properties of Pitton's type 2 beta-lactamase (SHV-1). Ann Inst Pasteur Microbiol. 1986 Jul-Aug;137B(1):19–27. doi: 10.1016/s0769-2609(86)80090-4. [DOI] [PubMed] [Google Scholar]
  8. Bergström S., Olsson O., Normark S. Common evolutionary origin of chromosomal beta-lactamase genes in enterobacteria. J Bacteriol. 1982 May;150(2):528–534. doi: 10.1128/jb.150.2.528-534.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Fisher J., Belasco J. G., Khosla S., Knowles J. R. beta-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry. 1980 Jun 24;19(13):2895–2901. doi: 10.1021/bi00554a012. [DOI] [PubMed] [Google Scholar]
  10. Jaurin B., Grundström T. ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4897–4901. doi: 10.1073/pnas.78.8.4897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kliebe C., Nies B. A., Meyer J. F., Tolxdorff-Neutzling R. M., Wiedemann B. Evolution of plasmid-coded resistance to broad-spectrum cephalosporins. Antimicrob Agents Chemother. 1985 Aug;28(2):302–307. doi: 10.1128/aac.28.2.302. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Levesque R. C., Medeiros A. A., Jacoby G. A. Molecular cloning and DNA homology of plasmid-mediated beta-lactamase genes. Mol Gen Genet. 1987 Feb;206(2):252–258. doi: 10.1007/BF00333581. [DOI] [PubMed] [Google Scholar]
  13. Matthew M., Hedges R. W., Smith J. T. Types of beta-lactamase determined by plasmids in gram-negative bacteria. J Bacteriol. 1979 Jun;138(3):657–662. doi: 10.1128/jb.138.3.657-662.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Matthew M. Plasmid-mediated beta-lactamases of Gram-negative bacteria: properties and distribution. J Antimicrob Chemother. 1979 Jul;5(4):349–358. doi: 10.1093/jac/5.4.349. [DOI] [PubMed] [Google Scholar]
  15. Medeiros A. A. Beta-lactamases. Br Med Bull. 1984 Jan;40(1):18–27. doi: 10.1093/oxfordjournals.bmb.a071942. [DOI] [PubMed] [Google Scholar]
  16. Medeiros A. A., Cohenford M., Jacoby G. A. Five novel plasmid-determined beta-lactamases. Antimicrob Agents Chemother. 1985 May;27(5):715–719. doi: 10.1128/aac.27.5.715. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Nugent M. E., Hedges R. W. The nature of the genetic determinant for the SHV-1 beta-lactamase. Mol Gen Genet. 1979 Oct 1;175(3):239–243. doi: 10.1007/BF00397222. [DOI] [PubMed] [Google Scholar]
  18. Pitton J. S. Mechanisms of bacterial resistance to antibiotics. Ergeb Physiol. 1972;65:15–93. doi: 10.1007/3-540-05814-1_2. [DOI] [PubMed] [Google Scholar]
  19. Sawai T., Yamagishi S., Mitsuhashi S. Penicillinases of Klebsiella pneumoniae and their phylogenetic relationship to penicillinases mediated by R factors. J Bacteriol. 1973 Sep;115(3):1045–1054. doi: 10.1128/jb.115.3.1045-1054.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sutcliffe J. G. Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3737–3741. doi: 10.1073/pnas.75.8.3737. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES