Linked Life Data

6967296

Source:http://linkedlifedata.com/resource/pubmed/id/6967296

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1980-9-26
pubmed:abstractText
A number of bacterial strains, each possessing a different aminoglycoside-modifying enzyme, were examined for susceptibility to sisomicin and gentamicin B and the semisynthetic derivatives 5-epi-sisomicin and 5-epi-gentamicin B. Although strains possessing AAC (6') or APH(3') enzymes were equally resistant to the 5-epi-compounds, those possessing AAC(3)-I, ANT(2"), or AAC(2') enzymes were much more sensitive to the 5-epi derivatives. Analysis of partially purified aminoglycoside-modifying enzymes from the strains showed that the 5-epi compounds were substrates even for those enzymes found in susceptible strains [AAC(3)-I, ANT(2"), and AAC(2')]. However, a more detailed study of the enzymes showed that they had much increased Km values for the 5-epi derivatives; the 5-epi compounds were much less effectively modified than the parent antibiotics. This confirms and extends the notion that enzymatic modification of aminoglycosides is not in itself sufficient to confer resistance to the drugs, but also that the modification must be efficient, as reflected in the Km values.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0066-4804
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
798-802
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
5-epi-Sisomicin and 5-epi-Gentamicin B: substrates for aminoglycoside-modifying enzymes that retain activity against aminoglycoside-resistant bacteria.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.