EC - Lauroyl-Kdo2-lipid IVA myristoyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
lauroyl-Kdo2-lipid IVA myristoyltransferase
Other names:
MsbB acyltransferase
lpxM (gene name)
myristoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-(dodecanoyl)-lipid IVA O-myristoyltransferase
Systematic name:
fatty acyl-[acyl-carrier protein]-α-Kdo-(2→4)-α-Kdo-(2→6)-(acyl)-[lipid IVA] O-acyltransferase



The enzyme is involved in the biosynthesis of the phosphorylated outer membrane glycolipid lipid A. It transfers an acyl group to the 3-O position of the 3R-hydroxyacyl already attached at the 2-O position of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for myristoyl (C14) acyl groups, giving the enzyme its previous accepted name. However, enzymes from different species accept highly variable substrates.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB


  1. Clementz, T., Zhou, Z., Raetz, C. R.
    Function of the Escherichia coli msbB gene, a multicopy suppressor of htrB knockouts, in the acylation of lipid A. Acylation by MsbB follows laurate incorporation by HtrB.
    J. Biol. Chem. 272 : 10353-10360 (1997). [PMID: 9099672]
  2. Dovala, D., Rath, C. M., Hu, Q., Sawyer, W. S., Shia, S., Elling, R. A., Knapp, M. S., Metzger, L. E.
    Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism.
    Proc Natl Acad Sci U S A 113 : E6064-E6071 (2016). [PMID: 27681620]

[EC created 2014]