EC - Kdo2-lipid IVA lauroyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
Kdo2-lipid IVA lauroyltransferase
Other names:
htrB (gene name)
dodecanoyl-[acyl-carrier protein]:α-Kdo-(2→4)-α-Kdo-(2→6)-lipid IVA O-dodecanoyltransferase
lauroyl-[acyl-carrier protein]:Kdo2-lipid IVA O-lauroyltransferase
(Kdo)2-lipid IVA lauroyltransferase
α-Kdo-(2→4)-α-(2→6)-lipid IVA lauroyltransferase
Systematic name:
dodecanoyl-[acyl-carrier protein]:Kdo2-lipid IVA O-dodecanoyltransferase



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 to the nitrogen of the non-reducing glucosamine molecule. The enzyme from the bacterium Escherichia coli is specific for lauryl (C12) 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., Bednarski, J. J., Raetz, C. R.
    Function of the htrB high temperature requirement gene of Escherchia coli in the acylation of lipid A: HtrB catalyzed incorporation of laurate.
    J. Biol. Chem. 271 : 12095-12102 (1996). [PMID: 8662613]
  2. Six, D. A., Carty, S. M., Guan, Z., Raetz, C. R.
    Purification and mutagenesis of LpxL, the lauroyltransferase of Escherichia coli lipid A biosynthesis.
    Biochemistry 47 : 8623-8637 (2008). [PMID: 18656959]
  3. McLendon, M. K., Schilling, B., Hunt, J. R., Apicella, M. A., Gibson, B. W.
    Identification of LpxL, a late acyltransferase of Francisella tularensis.
    Infect Immun 75 : 5518-5531 (2007). [PMID: 17724076]
  4. Fathy Mohamed, Y., Hamad, M., Ortega, X. P., Valvano, M. A.
    The LpxL acyltransferase is required for normal growth and penta-acylation of lipid A in Burkholderia cenocepacia.
    Mol Microbiol 104 : 144-162 (2017). [PMID: 28085228]

[EC created 2014]