PlsY belongs to the family of acyltransferases (EC 2.3.1.n3) and operates in the Bordetella avium glycerolipid synthesis pathway . Key features include:
Substrate specificity: Utilizes acyl-phosphate as the acyl donor (not acyl-CoA or acyl-ACP) .
Catalytic activity: Converts acyl-phosphate + G3P → LPA + inorganic phosphate .
Membrane topology: Contains five transmembrane segments, with conserved cytoplasmic motifs critical for substrate binding and catalysis .
Motif 1: Essential serine (Ser) and arginine (Arg) residues for catalysis .
Motif 2: Phosphate-binding loop with glycine residues critical for G3P binding .
Motif 3: Histidine (His) and asparagine (Asn) for structural integrity .
Recombinant PlsY from B. avium (strain 197N) is produced in E. coli systems for research applications. Key properties include:
ELISA and immunodetection: Recombinant PlsY is used as an antigen in immunological assays to study antibody responses .
Enzyme kinetics: Mutagenesis studies (e.g., glycine-to-alanine substitutions in Motif 2) reveal defects in Km for G3P binding .
Inhibition studies: Noncompetitive inhibition by palmitoyl-CoA highlights regulatory mechanisms .
Vaccine development: While not directly used in vaccines, B. avium recombinant proteins (e.g., ompA-Fc fusions) leverage similar expression systems (Pichia pastoris) to enhance immunogenicity .
Antimicrobial research: Understanding PlsY’s role in membrane biogenesis aids in targeting bacterial lipid metabolism for drug discovery .
PlsY differs from eukaryotic GPATs, which typically acylate the sn-1 position of G3P. In contrast, some plant GPATs (e.g., GPAT4/6) exhibit sn-2 preference and phosphatase activity .
KEGG: bav:BAV1982
STRING: 360910.BAV1982