EC Number   |
General Information |
Reference |
|---|
    2.7.4.2 | evolution |
Cinnamomum camphora PMK has 3 PMK protein family motifs and 1 ATP binding site Gly-Leu-Gly-Ser-Ser-Ala-Ala, and its 3 D structure contains a catalytic pocket structure, proving CcPMK as a member of PMK gene family |
760236 |
| 2.7.4.2 | evolution |
phosphomethoxylate kinase (PMK) is a member of the GHMP kinase superfamily. The GbPMK protein has four conserved domains and one conserved region of the GHMP kinase family. GbPMK possesses a conserved sequence structure and sequence characteristics. PMK phylogenetic and molecular evolution analyses |
759336 |
| 2.7.4.2 | evolution |
the enzyme belongs to the the GHMP kinase superfamily |
759656 |
| 2.7.4.2 | malfunction |
PMVK is a gene involved in the pathogenesis of disseminated superficial porokeratosis (DSP), a rare keratinization disorder of the epidermis, which is characterized by keratotic lesions with an atrophic center encircled by a prominent peripheral ridge. PMVK deficiency or abnormal keratinocyte apoptosis can lead to porokeratosis. The Arg138* genetic variant (nonsense mutation) is involved in the development of DSP in both families. Using HaCaT cells as models, it is revealed that this variant disturbs subcellular localization, expression, and solubility of PMVK, apparent apoptosis in and under the cornoid lamella of PMVK-deficient lesional tissues is observed, with incomplete differentiation of keratinocytes |
760138 |
| 2.7.4.2 | metabolism |
almost all eukaryotes, most of the MVA pathway-utilizing bacteria, and the archaea of the order Sulfolobales utilize mevalonate kinase (MVK), phosphomevalonate kinase (PMK), and diphosphomevalonate decarboxylase (DMD) for that purpose. The pathway that includes this set of enzymes is called the classical MVA pathway because it was discovered more than half a century ago |
-, 758668 |
| 2.7.4.2 | metabolism |
phosphomevalonate kinase catalyzes the rate-limiting step for biosynthesis of isopentenyl diphosphate from mevalonate |
710506 |
| 2.7.4.2 | metabolism |
the enzyme is a representative kinase in the mevalonate pathway |
759656 |
| 2.7.4.2 | more |
the phosphorylation reaction mechanism of phosphomevalonate kinase is studied by using molecular dynamics and hybrid QM/MM methods, the crystal structure of PMK in complex with its substrate (R)-5-phosphomevalonate (PMV) and AMPPNP-Mg2+ (PDB ID 3GON) is used as the initial structure. MD simulations are performed for the wild-type kinase and five variants, K9R, K9M, K101R, K101M, and A293T, respectively |
759656 |
| 2.7.4.2 | physiological function |
distinct from other GHMP kinases, PMK catalyzes the transfer of the gamma-phosphate of ATP to another negatively charged phosphate in the substrate. In addition, Mg2+ is only coordinated to the gamma-phosphoryl group of ATP in PMK, whereas it is coordinated to at least two phosphoryl groups of ATP in other GHMP kinases, structure-function analysis, detailed overview |
759656 |
| 2.7.4.2 | physiological function |
involved in terpenoid metabolism |
706809 |
