Properties of a Bifunctional Bacterial Antibiotic Resistance Enzyme That Catalyzes ATP-Dependent 2‘‘-Phosphorylation and Acetyl-CoA-Dependent 6‘-Acetylation of Aminoglycosides
An interesting enzyme confers resistance to a broad spectrum of aminoglycoside antibiotics primarily in Gram-positive bacteria. The enzyme was suggested to have two enzymic activities (phosphotransferase and acetyltransferase), based on the substrate profile and investigation of its gene with DNA pr...
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| Published in: | Journal of the American Chemical Society Vol. 119; no. 9; pp. 2317 - 2318 |
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| Main Authors: | , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
American Chemical Society
05-03-1997
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| Online Access: | Get full text |
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| Summary: | An interesting enzyme confers resistance to a broad spectrum of aminoglycoside antibiotics primarily in Gram-positive bacteria. The enzyme was suggested to have two enzymic activities (phosphotransferase and acetyltransferase), based on the substrate profile and investigation of its gene with DNA probes. We have purified this enzyme to apparent homogeneity in two chromatographic steps (cibacron blue and gentamicin-Sepharose columns). The enzyme turned over aminoglycosides with transfer of either the gamma - super(32)P-phosphate moiety from ATP or the [ super(3)H]-acetyl moiety from acetyl coenzyme A. |
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| Bibliography: | ark:/67375/TPS-6M40C62R-G istex:EB4FD442475FD35538F68E16F4B74C6D228C6DBA ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
| ISSN: | 0002-7863 1520-5126 |
| DOI: | 10.1021/ja964278w |