The substrate specificity of deacetoxycephalosporin C synthase ('expandase') of Streptomyces clavuligerus is extremely narrow
| Autor: | Aiqi Fang, Oscar Ferrero, Saul Wolfe, Michael Yu. Lebedev, Kiyoshi Maeda, José M. Luengo, Arnold L. Demain |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
biology Deacetoxycephalosporin-C synthase Streptomycetaceae Stereochemistry education Substrate (chemistry) Streptomyces clavuligerus Bioengineering biology.organism_classification Applied Microbiology and Biotechnology Biochemistry chemistry.chemical_compound Enzyme Biosynthesis chemistry mental disorders biology.protein Actinomycetales Magnesium ion psychological phenomena and processes Biotechnology |
| Zdroj: | Enzyme and Microbial Technology. 17:231-234 |
| ISSN: | 0141-0229 |
| Popis: | Cell-free extracts of Streptomyces clavuligerus contain the enzyme deacetoxycephalosporin C synthase (“expandase”), which catalyzes the oxidative ring expansion of the natural substrate δ- d -α-aminoadipyl-6-APA (penicillin N) into the primary cephalosporin, deacetoxycephalosporin C in the presence of magnesium ions, ferrous ions, ascorbate, and α-ketoglutarate. Eighteen unnatural side chain analogues of penicillin N were exposed to these reaction conditions. Only d -carboxymethylcysteinyl-6-APA was found to undergo ring expansion. Of special interest is the observation that adipyl-6-APA and m -carboxyphenylacetyl-6-APA were not expanded. |
| Databáze: | OpenAIRE |
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