 |
Online ISSN : 2349-8080 Issues : 12 per year Publisher : Excellent Publishers Email : editorinchiefijcrbp@gmail.com |
2Hubei Collaborative Innovation Center of Targeted Antitumor Drug, Jingmen, Hubei 448000, China
3College of Chemical Engineering and Pharmacy, Jingchu University of Technology, Jingmen, Hubei 448000, China
The phosphomevalonate kinase gene (PMK) is one of the core enzymes in the biosynthetic pathway of sesquiterpenoids and catalyzes the formation of mevalonate-5-diphosphate (MVAPP). In order to isolate and identify the PMK gene, a specific primer was designed based on the McPMK gene sequence in the transcriptome of Matricaria chamomilla. The full-length cDNA was 1782 bp of PMK gene and named McPMK (GenBank Accession No.MG778909). McPMK contains a 1479 bp open reading frame (ORF) encoding a total of 493 amino acids. McPMK proteins were analyzed online with molecular weights and isoelectric points of 53.58 KDa and 5.55, respectively. Amino acid multiple alignment showed that the McPMK encoded amino acid sequence is highly similar to other plant PMK proteins and has a GHMP kinase superfamily-specific ATP binding site. Phylogenetic tree analysis showed that McPMK clustered with Asteraceae PMKs in dicotyledonous species, and had the closest genetic relationship with Chamemelum nobile. The gene fragment of PMK amplified from M. chamomilla laid the foundation for the analysis of its function in the biosynthesis of terpenoids.
