9.B.31. The PlsY/YqiH (PlsY) Family
The integral membrane glycerol 3-phosphate (G3P) acyltransferase, PlsY, catalyses the committed and essential step in bacterial phospholipid biosynthesis by acylation of G3P, forming lysophosphatidic acid. The enzyme contains no known acyltransferase motifs, lacks eukaryotic homologs, and uses acyl-phosphate as acyl donor, as opposed to acyl-CoA or acyl-carrier protein, used by other acyltransferases. Several PlsY inhibitors are potential antimicrobials. Li et al. 2017 determined the crystal structure of PlsY at 1.48 A resolution, revealing a seven-transmembrane helix fold. Four additional substrate- and product-bound structures uncovered the atomic details of its relatively inflexible active site. A different acylation mechanism of 'substrate-assisted catalysis' was proposed that, unlike other acyltransferases, does not require a proteinaceous catalytic base to complete.
The PlsY or YgiH protein of 205 aas and 7 established TMSs. It plays a role in growth in complex media (Yoshimura et al. 2007). PlsY is glycerol 3-phosphate (G3P) acyltransferase which uses acyl-phosphate as the acyl donor. The 3-d structure is known (Li et al. 2017).
YgiH of E. coli (P60782)
Glycerol-3-phosphate acyltransferase, PlsY (Acyl-PO4 G3P acyltransferase) (Acyl-phosphate--glycerol-3-phosphate acyltransferase) (G3P acyltransferase) (GPAT) (EC 2.3.1.n3) (Lysophosphatidic acid synthase) (LPA synthase)
PlsY of Bacillus subtilis