Penicillinamidohydrolase in Escherichia coli. II. Synthesis of the enzyme, kinetics and specificity of its induction and the effect of O2
Language English Country United States Media print
Document type Journal Article
    PubMed
          
           1100492
           
          
          
    DOI
          
           10.1007/bf02878110
           
          
          
  
    Knihovny.cz E-resources
    
  
              
      
- MeSH
- Amidohydrolases biosynthesis MeSH
- Amides pharmacology MeSH
- Enzyme Induction MeSH
- Enzyme Repression MeSH
- Escherichia coli enzymology growth & development MeSH
- Phenoxyacetates pharmacology MeSH
- Phenylacetates pharmacology MeSH
- Kinetics MeSH
- Culture Media MeSH
- Oxygen pharmacology MeSH
- Penicillin Amidase biosynthesis MeSH
- Structure-Activity Relationship MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Amidohydrolases MeSH
- Amides MeSH
- Phenoxyacetates MeSH
- Phenylacetates MeSH
- Culture Media MeSH
- Oxygen MeSH
- Penicillin Amidase MeSH
The differential rate of synthesis of penicillinamidohydrolase (penicillin acylase -- EC 3.5.1.11) was studied in Escherichia coli growing in some chemically defined media and in a complex medium. The enzyme is synthesized at a constant rate only during the exponential phase of growth of cells. Its synthesis is induced most effectively (with respect to quantity) by phenylacetic acid. The induction lag of the enzyme synthesis in a medium with acetate corresponds to two generation times. The highest rate of the enzyme synthesis is reached in a medium containing phenylacetic acid as the only source of carbon and energy. The enzyme synthesis is fully repressed by an increased concentration of dissolved oxygen in the medium, even when Escherichia coli is cultivated in the medium with phenylacetic acid as the only carbon and energy source.
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