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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.


References associated with 9.B.31 family:

Li, Z., Y. Tang, Y. Wu, S. Zhao, J. Bao, Y. Luo, and D. Li. (2017). Structural insights into the committed step of bacterial phospholipid biosynthesis. Nat Commun 8: 1691. 29167463
Yoshimura, M., T. Oshima, and N. Ogasawara. (2007). Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. BMC Microbiol 7: 69. 17645809