On the compartmentation of isopentenyl diphosphate synthesis and utilization in plant cells
β Scribed by Klaus Kreuz; Hans Kleinig
- Book ID
- 104749433
- Publisher
- Springer-Verlag
- Year
- 1981
- Tongue
- English
- Weight
- 346 KB
- Volume
- 153
- Category
- Article
- ISSN
- 0032-0935
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β¦ Synopsis
Purified spinach chloroplast and daffodil chromoplast preparations do not use mevalonate, phosphomevalonate, and diphosphomevalonate for the synthesis of isopentenyl diphosphate. Isopentenyl diphosphate, on the other hand, is incorporated into plastidal polyprenoids in large amounts. In the presence of a cytoplasmic supernatant, however, mevalonate and the phosphomevalonates were incorporated into the plastidal polyprenoids in equally large amounts, which demonstrates that the enzymes mevalonate kinase (EC 2.7.1.36), phosphomevalonate kinase (EC 2.7.4.2), and diphosphomevalonate decarboxylase (EC4.1.1.33) are soluble cytoplasmic enzymes and that they apparently do not occur as isoenzymes within the plastids. The concept is developed that isopentenyl diphosphate is a central intermediate in plant polyprenoid formation which is channeled into several compartments for different biosynthetic pathways.
π SIMILAR VOLUMES
To investigate the unknown stereochemical course of the reaction catalyzed by the type-II isomerase, which interconverts isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), a sample of [1,2-13 C 2 ]-IPP stereospecifically labelled with 2 H at C(2) was prepared by incubating a D 2 O
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