| Autor: |
Smith MR; Department of Food Science, Agricultural University, Wageningen, The Netherlands., van den Tweel WJ, de Bont JA |
| Jazyk: |
angličtina |
| Zdroj: |
Bioorganic & medicinal chemistry [Bioorg Med Chem] 1994 Jul; Vol. 2 (7), pp. 589-93. |
| DOI: |
10.1016/0968-0896(94)85005-4 |
| Abstrakt: |
A bacterium (strain photoB) photoassimilated 3-mercapto-2-methylpropionate as sole source of sulphur with methacrylate accumulating in the medium. This was thought to be the product of a sulphur-lyase type enzyme attacking the 3-mercapto-2-methylpropionate. Detailed examination of the biochemistry of the utilization of 3-mercapto-2-methylpropionate showed however that the thiol was first activated to 3-mercapto-2-methylpropionyl CoA. It appeared that this CoA-derivative then served as the substrate for a sulphur-lyase type enzyme, with methacrylyl-CoA as product. Further metabolism was via beta-hydroxyisobutyryl-CoA and beta-hydroxyisobutyrate. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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