Stereospecific oxidation of aliphatic alcohols catalyzed by galactose oxidase
| Autor: | Barbara N. Alberti, Alexander M. Klibanov, Michael A. Marletta |
|---|---|
| Rok vydání: | 1982 |
| Předmět: |
Glycerol
chemistry.chemical_classification Biophysics Substrate (chemistry) Stereoisomerism 1-Propanol Cell Biology Galactose Oxidase Biochemistry Substrate Specificity chemistry.chemical_compound Enzyme Stereospecificity chemistry Mollusca Propylene Glycols Glyceraldehyde Galactose oxidase Galactose Organic chemistry Enantiomer Molecular Biology |
| Zdroj: | Biochemical and Biophysical Research Communications. 108:804-808 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(82)90900-7 |
| Popis: | The stereospecificity of galactose oxidase (EC 1.1.3.9) from Dactylium dendroides in the oxidation of simple three-carbon alcohols has been examined. The enzyme oxidizes glycerol to optically pure S(−)glyceraldehyde. In addition to this prochiral stereospecificity, galactose oxidase also exhibits enantiomeric stereospecificity in the oxidation of 3-halo-1,2-propanediols: the R isomer appears to be a better substrate than its S counterpart. The above stereochemistry of galactose oxidase-catalyzed oxidation of “unnatural” substrates, non-sugar alcohols, can be predicted on the basis of the conformation of the natural substrate of the enzyme, D-galactose. |
| Databáze: | OpenAIRE |
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