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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1996-8-22
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pubmed:abstractText |
Aminoglycoside antibiotics (AGs) with a free 2'-amino group were subjected to enzymatic N-acetylation using a cell free extract that contained an aminoglycoside 2'-N-acetyltransferase, AAC (2'), derived from a kasugamycin-producing strain of Streptomyces kasugaensis. TLC and antibiotic assay of the incubated reaction mixtures revealed that a modified compound retaining substantial antibiotic activity was formed from arbekacin (ABK), while modification of the other AGs resulted in the marked decrease in antibiotic activity. Structure determination following isolation from a large scale reaction mixture showed the modified ABK to be 2'-N-acetyl ABK. In addition, 2',6'-di-N-acetyl ABK was formed as a minor product. The same conversion also occurred with dibekacin (DKB) resulting in the formation of 2'-N-acetyl DKB and 2',6'-di-N-acetyl DKB. MIC determination showed antibacterial activity (1.56 approximately 3.13 micrograms/ml) of 2'-N-acetyl ABK against a variety of organisms. By contrast, 2'-N-acetyl DKB showed no substantial antibiotic activity. We believe 2'-N-acetyl ABK has the highest and broadest antibacterial activity, compared with known N-acetylated AGs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Aminoglycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Dibekacin,
http://linkedlifedata.com/resource/pubmed/chemical/habekacin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-8820
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
458-64
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8682723-Acetylation,
pubmed-meshheading:8682723-Acetyltransferases,
pubmed-meshheading:8682723-Acylation,
pubmed-meshheading:8682723-Aminoglycosides,
pubmed-meshheading:8682723-Anti-Bacterial Agents,
pubmed-meshheading:8682723-Dibekacin,
pubmed-meshheading:8682723-Microbial Sensitivity Tests,
pubmed-meshheading:8682723-Molecular Structure,
pubmed-meshheading:8682723-Streptomyces,
pubmed-meshheading:8682723-Structure-Activity Relationship
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pubmed:year |
1996
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pubmed:articleTitle |
Enzymatic 2'-N-acetylation of arbekacin and antibiotic activity of its product.
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pubmed:affiliation |
National Institute of Health, Tokyo, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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