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J. Biol. Chem., Vol. 263, Issue 31, 15880-15887, Nov, 1988
A Brisson-Noel, P Delrieu, D Samain and P Courvalin
Resistance to lincomycin by inactivation has been detected in numerous
clinical isolates of Staphylococcus; in crude extracts of Staphylococcus
haemolyticus BM4610 and Staphylococcus aureus BM4611, inactivation of
lincomycin and clindamycin requires the presence of a nucleoside
5'-triphosphate (ATP, GTP, CTP, or UTP) as nucleotidyl donor and Mg2+ as
cofactor. The biochemical mechanism of lincosaminide inactivation was
elucidated by determination of the structure of inactivated lincomycin and
clindamycin by physicochemical techniques, including UV absorption
spectrophotometry, 31P and 1H nuclear magnetic resonance, and periodate
oxidation. In the two strains, inactivation of lincomycin gave rise to
lincomycin 3-(5'-adenylate), whereas clindamycin was inactivated through
its conversion to clindamycin 4-(5'- adenylate). The gene linA' encoding
the 3-lincomycin, 4-clindamycin O- nucleotidyltransferase in S. aureus
BM4611 has been sequenced and displays 93% homology with the gene linA
encoding the 3-lincomycin, 4- clindamycin O-nucleotidyltransferase found in
S. haemolyticus BM4610. The two enzymes are 161 amino acids long and differ
by 14 amino acid substitutions.
Inactivation of lincosaminide antibiotics in Staphylococcus. Identification of lincosaminide O-nucleotidyltransferases and comparison of the corresponding resistance genes
Unite des Agents Antibacteriens, Centre National de la Recherche Scientifique UA 271, Institut Pasteur, Paris, France.
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