EC Number   |
General Information |
Reference |
|---|
    4.1.1.33 | malfunction |
site-directed mutagenesis on Asp281 creates mutants that only show diphosphomevalonate 3-kinase activity, demonstrating that the residue is required in the process of phosphate elimination/decarboxylation, rather than in the preceding phosphorylation step |
-, 759486 |
| 4.1.1.33 | metabolism |
the enzyme catalyzes a reaction of the classical mevalonate pathway |
-, 722571 |
| 4.1.1.33 | metabolism |
the enzyme is implicated in latex metabolism. Rubber yields and/or yield characteristics are not significantly correlated with enzyme expression levels |
758969 |
| 4.1.1.33 | more |
the conserved aspartate residue, Asp281, shows inability for proton abstraction. Substrate-complex structures of DMD and M3K (EC 2.7.1.185), overview |
-, 759486 |
| 4.1.1.33 | physiological function |
gene is able to complement the growth defect of a Saccharomyces cervisiae mevalonete diphosphate decarboxylase mutant on YGPal medium |
-, 728280 |
| 4.1.1.33 | physiological function |
gene is able to functionally complement mevalonate 5-diphosphate decarboxylase deletion mutants in the yeast Saccharomyces cerevisiae |
728536 |
| 4.1.1.33 | physiological function |
investigation of the role of mevalonate diphospho decarboxylase in viral replication |
706892 |
| 4.1.1.33 | physiological function |
the biosynthesis of isopentenyl diphosphate, a fundamental precursor for isoprenoids, via the mevalonate pathway is completed by diphosphomevalonate decarboxylase. This enzyme catalyzes the formation of isopentenyl diphosphate through the ATP-dependent phosphorylation of the 3-hydroxyl group of (R)-5-diphosphomevalonate followed by decarboxylation coupled with the elimination of the 3-phosphate group. Involvement of a long predicted intermediate, (R)-3-phospho-5-diphosphomevalonate, in the reaction of the enzyme |
-, 759486 |
