Penicillinamidohydrolase in Escherichia coli. II. Synthesis of the enzyme, kinetics and specificity of its induction and the effect of O2
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
1100492
DOI
10.1007/bf02878110
Knihovny.cz E-zdroje
- MeSH
- amidohydrolasy biosyntéza MeSH
- amidy farmakologie MeSH
- enzymová indukce MeSH
- enzymová represe MeSH
- Escherichia coli enzymologie růst a vývoj MeSH
- fenoxyacetáty farmakologie MeSH
- fenylacetáty farmakologie MeSH
- kinetika MeSH
- kultivační média MeSH
- kyslík farmakologie MeSH
- penicilinamidasa biosyntéza MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- amidohydrolasy MeSH
- amidy MeSH
- fenoxyacetáty MeSH
- fenylacetáty MeSH
- kultivační média MeSH
- kyslík MeSH
- penicilinamidasa 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.
Zobrazit více v PubMed
Can J Microbiol. 1967 Jul;13(7):761-9 PubMed
Appl Microbiol. 1964 May;12:185-7 PubMed
Can J Microbiol. 1967 Feb;13(2):147-57 PubMed
Folia Microbiol (Praha). 1975;20(3):224-30 PubMed
Mikrobiologiia. 1967 Sep-Oct;36(5):912-7 PubMed
Prikl Biokhim Mikrobiol. 1972 Sep-Oct;8(5):559-61 PubMed
Cell aggregates of Escherichia coli with benzylpenicillin amidase activity
