Abstract
It is well known (1) that one of the processes of inactivation of aminoglycosides by some bacteria is a structural modification of these antibiotics, e.g. N-acetylation, o-adenylylation, o-phosphorylation. The study of the structure activity relationship requires the preparation of specifically modified aminoglycosides at one of the amino or hydroxyl functions. The only way to obtain such specificity is by enzymatic reactions. We therefore used enzymes isolated from resisting bacterial strains, performing specific modification of aminoglycosides. We thus modified Gentamicin, Sisomicin and Tobramycin.
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References
PRICE, K.E., GODFREY, J.C. & KAWAGUCHI, H. in “Advances in Applied Microbiology,” vol. 18 ( W.W. Umbreit, ed.), Academic Press, New York, 1974, p. 191.
BROUN, G., THOMAS, D., GELFF, G., DOMURADO, D., BERJONNEAU, A.M. & GUILLON, C. Bi.otechnot. Bioeng. 15: 359, 1973.
LE GOFFIC, F., SICSIC, S. & VINCENT, C. Tetnahednon Ltns. 33: 2845, 1976.
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© 1978 Plenum Press, New York
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Le Goffic, F., Le Bigot, J.F., Sicsic, S., Vincent, C. (1978). Hemisynthesis of Aminoglycosides. In: Broun, G.B., Manecke, G., Wingard, L.B. (eds) Enzyme Engineering. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6985-1_34
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DOI: https://doi.org/10.1007/978-1-4684-6985-1_34
Publisher Name: Springer, Boston, MA
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