EC Number   |
Protein Variants |
Reference |
|---|
    2.7.1.185 | D281A |
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation |
-, 759486 |
| 2.7.1.185 | D281N |
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation |
-, 759486 |
| 2.7.1.185 | D281T |
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation |
-, 759486 |
| 2.7.1.185 | D281V |
site-directed mutagenesis, the mutant only shows reduced diphosphomevalonate 3-kinase activity compared to wild-type, but is inactive in the process of phosphate elimination/decarboxylation |
-, 759486 |
| 2.7.1.185 | E140A |
site-directed mutagenesis, inactive mutant |
-, 758668 |
| 2.7.1.185 | E140G |
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate |
-, 758668 |
| 2.7.1.185 | E140S |
site-directed mutagenesis, the mutation results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate |
-, 758668 |
| 2.7.1.185 | L18A |
kcat/KM for (R)-mevalonate is 4.4% compared to the wild-type value |
730902 |
| 2.7.1.185 | more |
substrate-interacting glutamate residue E140 of Thermoplasma acidophilum mevalonate 3-kinase is replaced by smaller amino acids, including its counterparts in diphosphomevalonate decarboxylase and phosphomevalonate decarboxylase, with the aim of altering substrate specificity. These single amino acid mutations results in the conversion of mevalonate 3-kinase into 5-phosphomevalonate 3-kinase, which can synthesize 3,5-bisphosphomevalonate from 5-phosphomevalonate. The mutants catalyzing the hitherto undiscovered reaction enables the construction of an artificial mevalonate pathway in Escherichia coli cells, as is demonstrated by the accumulation of lycopene, a red carotenoid pigment. Neither wild-type TacM3K nor any mutants show reactivity toward MVA 5-diphosphate. Alternative MVA pathway II overview. Constructed plasmids and strains, overview |
-, 758668 |
| 2.7.1.185 | R185A |
mutation results in no detectable activity |
730902 |
