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. 1970 Jan;1(1):109–119. doi: 10.1128/iai.1.1.109-119.1970

Enzymatic Adenylylation of Streptomycin and Spectinomycin by R-Factor-Resistant Escherichia coli

R Benveniste 1, T Yamada 1, J Davies 1
PMCID: PMC415862  PMID: 16557683

Abstract

A resistance (R) factor- containing strain of Escherichia coli which is known to inactivate streptomycin by adenylylation has been shown to be spectinomycin resistant. An osmotic shockate of this strain catalyzes the formation of the biologically inactive spectinomycin adenylate, in which the adenylyl residue is probably attached to a d-threo methylamino alcohol moiety of spectinomycin. Both the streptomycin and spectinomycin adenylylating activities show the same temperature inactivation profile, and both are present in a protein fraction purified for the streptomycin inactivating enzyme. Mutants obtained from this strain which were sensitive to either spectinomycin or streptomycin were shown to lack both enzymatic activities when tested in vitro. Revertants of these mutants selected for recovery of either streptomycin resistance or spectinomycin resistance regain both activities. Therefore, we conclude that the inactivation of the two drugs is catalyzed by the same enzyme. Examination of a number of R factor-carrying strains has shown that those strains which are resistant to streptomycin and spectinomycin contain the adenylylating enzyme, whereas strains resistant to streptomycin but sensitive to spectinomycin inactivate streptomycin by phosphorylation.

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Selected References

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

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