Undecaprenyl diphosphate synthase reaction with artificial substrate homologues — novel behavior in the termination of prenyl chain elongation
✍ Scribed by Shin-ichi Ohnuma; Michio Ito; Tanetoshi Koyama; Kyozo Ogura
- Publisher
- Elsevier Science
- Year
- 1989
- Tongue
- French
- Weight
- 870 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0040-4020
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✦ Synopsis
E)-3-Methyl-3-pentenyl diphosphate acted as an artificial homoallylic substrate in the reaction with several allylic diphosphates catalyzed by undecaprenyl diphosphate synthase of Bacillus subtilis. The synthase reaction with the artificial substrate proceeded in the same stereochemical manner as that with the natural homoallylic substrate, isopentenyl diphosphate, but it had a full stop at the stage where a single condensation of the C -homologue with an 6 allylic primer is completed to form a chiral prenyl diphosphate with an extra methyl group at the 4-position.
Allylic diphosphates that each have an extra methyl group at the 4-position were not accepted as substrates for this enzyme even when isopentenyl diphosphate was the homoallylic substrate.