Substrate specificity of the paraffin hydroxylase of Pseudomonas aeruginosa
| Autor: | J. C. van Ravenswaay Claasen, A. C. van der Linden |
|---|---|
| Rok vydání: | 1971 |
| Předmět: |
chemistry.chemical_classification
Chromatography Gas Strain (chemistry) Stereochemistry Hydrolases Benzene Cycloparaffins General Medicine Microbiology Culture Media Hydroxylation chemistry.chemical_compound Methyl carbon chemistry Paraffin Enzyme Induction Alkanes Pseudomonas aeruginosa Benzene Derivatives Substrate specificity Molecule Alkylbenzenes Molecular Biology Alkyl Isopropyl |
| Zdroj: | Antonie van Leeuwenhoek. 37(3) |
| ISSN: | 0003-6072 |
| Popis: | The paraffin hydroxylating enzyme system isolated fromPseudomonas aeruginosa (strain 473) grown onn-heptane has been studied with respect to its substrate specificity. It has been found that cell-free extracts of this organism can hydroxylate a wide variety of hydrocarbons. In order to function as substrates, molecules should be able to assume a more or less planar conformation. The compounds used in this study can be divided into three classes: (a) alkanes, (b) alkylbenzenes and (c) (alkyl)cycloalkanes. In each of these groups hydroxylation occurs at a specific site in the molecule. Noteworthy is the hydroxylation of isopropyl groups at a methyl carbon and that of monoalkylcyclohexanes at the 4-transposition. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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