Abstract
Mevalonate pyrophosphate decarboxylase (MPD) is a key enzyme in terpenoid biosynthesis. MPD plays an important role in the upstream regulation of secondary plant metabolism. However, studies on the MPD gene are relatively very few despite its importance in plant metabolism. Currently, no systematic analysis has been conducted on the MPD gene in plants under the order Apiales, which comprises important medicinal plants such as Panax ginseng and Panax notoginseng. This study sought to explore the structural characteristics of the MPD gene and the effect of adaptive evolution on the gene by comparing and analyzing MPD gene sequences of different campanulids species. For that, phylogenetic and adaptive evolution analyses were carried out using sequences for 11 Campanulids species. MPD sequence characteristics of each species were then analyzed, and the collinearity analysis of the genes was performed. As a result, a total of 21 MPD proteins were identified in 11 Campanulids species through BLAST analysis. Phylogenetic analysis, physical and chemical properties prediction, gene family analysis, and gene structure prediction showed that the MPD gene has undergone purifying selection and exhibited highly conserved structure. Analysis of physicochemical properties further showed that the MPD protein was a hydrophilic protein without a transmembrane region. Moreover, collinearity analysis in Apiales showed that MPD gene on chromosome 2 of D. carota and chromosome 1 of C. sativum were collinear. The findings showed that MPD gene is highly conserved. This may be a common characteristic of all essential enzymes in the biosynthesis pathways of medicinal plants. Notably, MPD gene is significantly affected by environmental factors which subsequently modulate its expression. The current study’s findings provide a basis for follow-up studies on MPD gene and key enzymes in other medicinal plants.
Highlights
Mevalonate pyrophosphate decarboxylase (MPD) gene is significantly affected by environmental factors which subsequently modulate its expression
Mevalonate pyrophosphate decarboxylase (MPD) is an enzyme that belongs to the Galactokinase-Homoserine kinase (GHMP) superfamily
Cynara cardunculus var. scolymus, Lactuca sativa, Mikania micrantha, Helianthus annuus, Taraxacum kok saghyz, Artemisia annua, and Chrysanthemum nankingense were grouped into Asteraceae, whereas D. carota and C. sativum clustered into Apiaceae
Summary
Mevalonate pyrophosphate decarboxylase (MPD) is an enzyme that belongs to the Galactokinase-Homoserine kinase (GHMP) superfamily. It plays a key role in the Mevalonate (MVA) pathway and is the least studied enzyme in the GHMP superfamily [1,2]. In silico/computational analysis of MPD gene families in Campanulids 1023 conserved across different species. MPD comprises two identical subunits in yeast: a monomer and a fissure structure. Three reverse parallel β-folds separate the α-helix in the monomer, and the fissure structure is implicated in ATP binding and comprises conserved amino acid residues [4]. The gene that encodes MPD is ubiquitous in animals, plants, and microorganisms such as Panax ginseng [5], Ganoderma lucidum [6], Bacopa monniera [7], Homo sapiens [8], Sus scrofa [9], Enterococcus faecalis [10], and Bifidobacterium bifidus [11]
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