Recombinant Burkholderia cenocepacia Phosphatidylserine decarboxylase proenzyme (psd)
Description
Introduction
Phosphatidylserine decarboxylase (PSD) is a critical enzyme in microbial lipid metabolism, catalyzing the conversion of phosphatidylserine (PtdSer) to phosphatidylethanolamine (PtdEtn). The recombinant form of this enzyme from Burkholderia cenocepacia (strain J2315) has garnered attention for its role in bacterial membrane biosynthesis and potential applications in biotechnology. This article synthesizes available data on the psd proenzyme, including its biochemical properties, structural features, and research implications.
Biochemical Function
The psd proenzyme is a key component of the phospholipid biosynthesis pathway in B. cenocepacia. Its primary function is to decarboxylate PtdSer, a precursor lipid, to produce PtdEtn, a major constituent of bacterial membranes. This reaction is essential for maintaining membrane integrity and cellular homeostasis. The enzyme is expressed as a proenzyme (preproenzyme) that undergoes processing to form its active mature form.
| Property | Description |
|---|---|
| Enzymatic Activity | Catalyzes PtdSer → PtdEtn conversion via decarboxylation |
| Protein Length | Full-length proenzyme: 181 amino acids |
| Expression Host | Yeast (Saccharomyces cerevisiae) and E. coli |
| Purification | Tris/PBS-based buffer with 6% trehalose for stability |
Role in Pathogenicity
While psd itself is not directly linked to virulence, its role in membrane lipid homeostasis may indirectly support B. cenocepacia’s survival in cystic fibrosis (CF) lung environments. Lipid metabolism pathways, including PtdEtn biosynthesis, are critical for bacterial persistence in nutrient-limited niches . Additionally, lipid remodeling enzymes like psd may contribute to biofilm formation and immune evasion, as seen in other CF pathogens .
Biotechnological Uses
The recombinant psd enzyme is used in studies of lipid metabolism and as a tool for synthesizing phospholipid precursors. Its expression in heterologous hosts (e.g., yeast and E. coli) facilitates large-scale production for biochemical assays.
Targeted Antimicrobial Development
Metabolic network reconstructions of B. cenocepacia highlight lipid biosynthesis as a potential therapeutic target . Inhibitors of psd or related enzymes could disrupt membrane synthesis, offering a novel approach to treating multidrug-resistant infections .
Product Specs
Target Background
KEGG: bcm:Bcenmc03_2285
