| Autor: | Charles A. Fewson, David J. Gillooly |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
biology Arginine Stereochemistry Perillyl alcohol Active site Bioengineering General Medicine biology.organism_classification Applied Microbiology and Biotechnology chemistry.chemical_compound Enzyme chemistry Benzyl alcohol biology.protein Organic chemistry Acinetobacter calcoaceticus Site-directed mutagenesis Histidine Biotechnology |
| Zdroj: | Biotechnology Letters. 20:325-327 |
| ISSN: | 0141-5492 |
| DOI: | 10.1023/a:1005306825491 |
| Popis: | Benzyl alcohol dehydrogenase from Acinetobacter calcoaceticus oxidises a wide range of aromatic and other cyclic alcohols and it has high specificity constants for these substrates, but it does not oxidise short- or long-chain aliphatic alcohols. Mutation of an active-site arginine to a histidine can switch the substrate specificity of the enzyme so that it has a very much greater preference for perillyl alcohol than for benzyl alcohol. © Rapid Science Ltd. 1998 |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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