Literature DB >> 2559963

Biochemical aspects of the resistance to nourseothricin (streptothricin) of Escherichia coli strains.

G Seltmann1.   

Abstract

In most cases Escherichia coli strains phenotypically resistant against nourseothricin (streptothricin) harbour a plasmid which codes for an acetyltransferase. This enzyme transfers an acetyl group from acetyl-coenzyme A to an amino group of the beta-lysine (peptide) chain of the antibiotic, thus inactivating it. Additionally, the penetrability for nourseothricin of the cell wall is drastically reduced in a high percentage of the resistant strains. Both resistance mechanisms seem to be independent of each other.

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Year:  1989        PMID: 2559963     DOI: 10.1002/jobm.3620290820

Source DB:  PubMed          Journal:  J Basic Microbiol        ISSN: 0233-111X            Impact factor:   2.281


  2 in total

1.  Enantiomeric free radicals and enzymatic control of stereochemistry in a radical mechanism: the case of lysine 2,3-aminomutases.

Authors:  E Behshad; F J Ruzicka; S O Mansoorabadi; D Chen; G H Reed; P A Frey
Journal:  Biochemistry       Date:  2006-10-24       Impact factor: 3.162

2.  Lysine-2,3-aminomutase and beta-lysine acetyltransferase genes of methanogenic archaea are salt induced and are essential for the biosynthesis of Nepsilon-acetyl-beta-lysine and growth at high salinity.

Authors:  K Pflüger; S Baumann; G Gottschalk; W Lin; H Santos; V Müller
Journal:  Appl Environ Microbiol       Date:  2003-10       Impact factor: 4.792

  2 in total

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