Letter | Published:

Microbial Degradation of Cephalosporin C

Abstract

THE antibiotic, cephalosporin C, is closely related to the penicillin family and displays the same mode of action1. Although cephalosporin C possesses the β-lactam ring—the substrate site of penicillinase action—it is resistant to this enzyme and, in fact, acts as a competitive inhibitor. It is, however, attacked by a ‘cephalosporinase’ found in crude preparations of penicillinase from Bacillus cereus2 and by a citrus acetyl esterase3. Although little is known about the site of attack by cephalosporinase, its action causes inactivation of the antibiotic with the loss of 260 mµ absorption and liberation of one acidic group. The esterase converts cephalosporin C to deacetylcephalosporin C, which retains the properties of ultra-violet absorption and resistance to penicillinase but which is a less-active antibiotic. We have now found that these two enzymatic activities are present in many bacteria and actinomycetes but not in the moulds examined.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Abraham, E. P., and Newton, G. G. F., Endeavour, 20, 92 (1961).

  2. 2

    Newton, G. G. F., and Abraham, E. P., Biochem. J., 62, 651 (1956).

  3. 3

    D'A. Jeffery, J., Abraham, E. P., and Newton, G. G. F., Biochem. J., 81, 591 (1961).

  4. 4

    Gots, J. S., Science, 102, 309 (1945).

Download references

Author information

Rights and permissions

Reprints and Permissions

About this article

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.