EC 2.3.1.191 - UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.191

Names

Accepted name:
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
Other names:
UDP-3-O-acyl-glucosamine N-acyltransferase
LpxD
acetyltransferase LpxD
acyl-ACP:UDP-3-O-(3-hydroxyacyl)-GlcN N-acyltransferase
firA
UDP-3-O-[3-hydroxymyristoyl]-D-glucosamine N-acyltransferase
UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase
(3R)-3-hydroxymyristoyl-[acyl-carrier protein]:UDP-3-O-[(3R)-hydroxymyristoyl]-α-D-glucosamine N-acyltransferase
Systematic name:
(3R)-3-hydroxyacyl-[acyl-carrier protein]:UDP-3-O-[(3R)-hydroxyacyl]-α-D-glucosamine N-acyltransferase

Reaction

Comments:

The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (3R)-3-hydroxytetradecanoyl-[acyl-carrier protein] [3], but it does not an absolute specificity for 14-carbon hydroxy fatty acids, as it can transfer other fatty acids, including odd-chain fatty acids, if they are available to the organism [5].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0103118
UniProtKB/Swiss-Prot: (330) [show] [UniProt]

References

  1. Bartling, C. M., Raetz, C. R.
    Crystal structure and acyl chain selectivity of Escherichia coli LpxD, the N-acyltransferase of lipid A biosynthesis.
    Biochemistry 48 : 8672-8683 (2009). [PMID: 19655786]
  2. Buetow, L., Smith, T. K., Dawson, A., Fyffe, S., Hunter, W. N.
    Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis.
    Proc. Natl. Acad. Sci. USA 104 : 4321-4326 (2007). [PMID: 17360522]
  3. Bartling, C. M., Raetz, C. R.
    Steady-state kinetics and mechanism of LpxD, the N-acyltransferase of lipid A biosynthesis.
    Biochemistry 47 : 5290-5302 (2008). [PMID: 18422345]
  4. Kelly, T. M., Stachula, S. A., Raetz, C. R., Anderson, M. S.
    The firA gene of Escherichia coli encodes UDP-3-O-(R-3-hydroxymyristoyl)-glucosamine N-acyltransferase. The third step of endotoxin biosynthesis.
    J. Biol. Chem. 268 : 19866-19874 (1993). [PMID: 8366125]
  5. Bainbridge, B. W., Karimi-Naser, L., Reife, R., Blethen, F., Ernst, R. K., Darveau, R. P.
    Acyl chain specificity of the acyltransferases LpxA and LpxD and substrate availability contribute to lipid A fatty acid heterogeneity in Porphyromonas gingivalis.
    J. Bacteriol. 190 : 4549-4558 (2008). [PMID: 18456814]
  6. Badger, J., Chie-Leon, B., Logan, C., Sridhar, V., Sankaran, B., Zwart, P. H., Nienaber, V.
    Structure determination of LpxD from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii.
    Acta Crystallogr Sect F Struct Biol Cryst Commun 69 : 6-9 (2013). [PMID: 23295477]
  7. Kroeck, K. G., Sacco, M. D., Smith, E. W., Zhang, X., Shoun, D., Akhtar, A., Darch, S. E., Cohen, F., Andrews, L. D., Knox, J. E., Chen, Y.
    Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography.
    Sci Rep 9 : 15450 (2019). [PMID: 31664082]

[EC 2.3.1.191 created 2010]