Zobrazeno 1 - 10
of 10
pro vyhledávání: '"G O, Daumy"'
Publikováno v:
Protein Science. 4:433-441
Two isoforms of the heterodimeric enzyme penicillin G acylase (EC 3.5.1.11) from Providencia rettgeri ATCC 31052 (strain Bro1) were purified to near homogeneity. The isoforms exhibited comparable enzymatic activities but differed slightly in the mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9704b96646833a3350004003658e7d92
https://doi.org/10.1002/pro.5560040310
https://doi.org/10.1002/pro.5560040310
Publikováno v:
Biochemistry. 39(24)
Protein-protein interactions (PPI) are a ubiquitous mode of transmitting signals in cells and tissues. We are testing a stepwise, generic, structure-driven approach for finding low molecular weight inhibitors of protein-protein interactions. The appr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f667974e6a5f9083462465978da08540
https://pubmed.ncbi.nlm.nih.gov/10852706
https://pubmed.ncbi.nlm.nih.gov/10852706
Publikováno v:
Biochemical pharmacology. 52(6)
In vitro pharmacologic measures of drug specificity are well established, i.e. drug interaction with a specific target such as an enzyme, receptor, or ion channel. However, in vitro measures of drug selectivity, defined as effects on secondary target
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::88557afa9f548546f5d13ab8f5bda39d
https://pubmed.ncbi.nlm.nih.gov/8781511
https://pubmed.ncbi.nlm.nih.gov/8781511
Publikováno v:
Journal of Bacteriology. 141:293-296
Mutans of Pseudomonas testosteroni were isolated for their inability to grow on m-hydroxybenzoate as sole carbon source. These mutants hydroxylated m-hydroxybenzoate for form 2,3-dihydroxybenzoate in high yeilds. The bioconversion described in this r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c9d73947dd54c4875e812ba861607a1
https://doi.org/10.1128/jb.141.1.293-296.1980
https://doi.org/10.1128/jb.141.1.293-296.1980
Publikováno v:
Journal of Bacteriology. 163:1279-1281
Penicillin G acylase from Proteus rettgeri is an 80,000- to 90,000-dalton enzyme composed of two nonidentical subunits. Both subunits were required for enzymatic activity. The 65,000-dalton beta subunit contained a phenylmethylsulfonyl fluoride-sensi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddbd97f7f67d4702280b0b6384f862c5
https://doi.org/10.1128/jb.163.3.1279-1281.1985
https://doi.org/10.1128/jb.163.3.1279-1281.1985
The penicillin G acylase genes from the Proteus rettgeri wild type and from a hyperproducing mutant which is resistant to succinate repression were cloned in Escherichia coli K-12. Expression of both wild-type and mutant P. rettgeri acylase genes in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaf108c12de7bec312892db67e21f4b2
https://europepmc.org/articles/PMC213471/
https://europepmc.org/articles/PMC213471/
Seventeen mutants of Pseudomonas putida that were unable to grow on threonine as nitrogen source owing to a lack of threonine dehydratase were isolated, and all were found to be unable to synthesize active urocanase. Spontaneous revertants selected f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::508f405dcfdd66d58418637877189773
https://europepmc.org/articles/PMC245907/
https://europepmc.org/articles/PMC245907/
Autor:
A. S. McColl, G. O. Daumy
Benzoate was established as the inducer of a unique 3-hydroxybenzoate 2-hydroxylase activity found in a Pseudomonas testosteroni mutant which is unable to grow on m -hydroxybenzoate as its sole source of carbon and energy.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0f77cae778944e01be6c242a2a50c9b
https://europepmc.org/articles/PMC216637/
https://europepmc.org/articles/PMC216637/
Publikováno v:
Journal of bacteriology. 163(3)
Proteus rettgeri and Escherichia coli W were shown to express structurally different penicillin G acylases. The enzymes had similar substrate specificity but differed in molecular weight, isoelectric point, and electrophoretic mobility in polyacrylam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::585fc52b7bfed212f9a4ecd0ed0a6f47
https://pubmed.ncbi.nlm.nih.gov/3897200
https://pubmed.ncbi.nlm.nih.gov/3897200
Publikováno v:
Biochimica et biophysica acta. 258(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e7536c71000eeb226c6c6a6f623a9490
https://pubmed.ncbi.nlm.nih.gov/4400493
https://pubmed.ncbi.nlm.nih.gov/4400493