The inhibition of murein synthesis in staphylococcus aureus by the antibiotic tetaine

tetaine inhibits the incorporation of 3H-Ala and 3H-Lys to murein of S. aureus/Oxford/. The inhibition occurs possibly at the level of incorporation of L-Ala to UDP-Mur-NAc, as in the presence of tetaine nucleotide precursors of murein synthesis were radioactive due to 3H-uridine and not 3H-Ala or 3...

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Published inBiochemical and biophysical research communications Vol. 55; no. 4; pp. 1147 - 1155
Main Authors Chmara, H., Borowski, E.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 19.12.1973
Subjects
Alanine - metabolism
Anti-Bacterial Agents - pharmacology
Biological Transport - drug effects
Chromatography, Paper
Cycloserine - pharmacology
D-cyclo
D-cycloserine
Dipeptides - biosynthesis
Lipids - biosynthesis
Lysine - metabolism
Meth
methicillin
Methicillin - pharmacology
Muramic Acids
Oligopeptides - pharmacology
Peptide Synthases - antagonists & inhibitors
Peptidoglycan - biosynthesis
Staphylococcus - drug effects
Staphylococcus - metabolism
Tet
tetaine
Tritium
UDP-Mur NAc
Uridine Diphosphate Sugars
uridine diphospho N-acetylmuramic acid
Vanco
vancomycin
Vancomycin - pharmacology
Meth
Tet
D-cyclo
UDP-Mur NAc
Vanco
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Abstract tetaine inhibits the incorporation of 3H-Ala and 3H-Lys to murein of S. aureus/Oxford/. The inhibition occurs possibly at the level of incorporation of L-Ala to UDP-Mur-NAc, as in the presence of tetaine nucleotide precursors of murein synthesis were radioactive due to 3H-uridine and not 3H-Ala or 3H-Lys. The availability of alanine is not effected as tetaine does not influence its transport through the membrane. In the cell-free system tetaine decreases the activity of partially purified L-alanine adding enzyme. Tetaine is transported through the cell membrane by dipeptide carrier.
AbstractList tetaine inhibits the incorporation of 3H-Ala and 3H-Lys to murein of S. aureus/Oxford/. The inhibition occurs possibly at the level of incorporation of L-Ala to UDP-Mur-NAc, as in the presence of tetaine nucleotide precursors of murein synthesis were radioactive due to 3H-uridine and not 3H-Ala or 3H-Lys. The availability of alanine is not effected as tetaine does not influence its transport through the membrane. In the cell-free system tetaine decreases the activity of partially purified L-alanine adding enzyme. Tetaine is transported through the cell membrane by dipeptide carrier.
Author Borowski, E.
Chmara, H.
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CitedBy_id crossref_primary_10_1016_0167_4781_85_90104_6
crossref_primary_10_1007_BF00408022
crossref_primary_10_1016_0167_4838_84_90106_7
crossref_primary_10_1016_0006_291X_78_91532_2
Cites_doi 10.1016/S0021-9258(19)73808-3
10.7164/antibiotics.26.184
10.1128/JB.110.1.35-40.1972
10.1016/0003-2697(60)90025-7
10.1128/JB.109.1.326-335.1972
10.1016/0006-291X(73)90654-2
10.1128/JB.108.3.1235-1243.1971
10.1128/JB.91.1.449-460.1966
10.1146/annurev.bi.40.070171.002145
10.1016/S0021-9258(18)65049-5
10.1016/S0021-9258(18)94507-2
10.1128/JB.110.3.935-944.1972
10.1128/AAC.2.6.485
10.1128/JB.108.1.20-29.1971
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Keywords Meth
Tet
D-cyclo
UDP-Mur NAc
Vanco
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Snippet tetaine inhibits the incorporation of 3H-Ala and 3H-Lys to murein of S. aureus/Oxford/. The inhibition occurs possibly at the level of incorporation of L-Ala...
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elsevier
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SubjectTerms Alanine - metabolism
Anti-Bacterial Agents - pharmacology
Biological Transport - drug effects
Chromatography, Paper
Cycloserine - pharmacology
D-cyclo
D-cycloserine
Dipeptides - biosynthesis
Lipids - biosynthesis
Lysine - metabolism
Meth
methicillin
Methicillin - pharmacology
Muramic Acids
Oligopeptides - pharmacology
Peptide Synthases - antagonists & inhibitors
Peptidoglycan - biosynthesis
Staphylococcus - drug effects
Staphylococcus - metabolism
Tet
tetaine
Tritium
UDP-Mur NAc
Uridine Diphosphate Sugars
uridine diphospho N-acetylmuramic acid
Vanco
vancomycin
Vancomycin - pharmacology
Title The inhibition of murein synthesis in staphylococcus aureus by the antibiotic tetaine
URI https://dx.doi.org/10.1016/S0006-291X(73)80015-4
https://www.ncbi.nlm.nih.gov/pubmed/4771988
https://search.proquest.com/docview/82147830
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