IntEnz

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

IntEnz Enzyme Nomenclature
EC 2.3.1.191

Names

Reaction

• 17817 [IUBMB]
  (3R)-hydroxytetradecanoyl-[ACP]

  (3R)-hydroxytetradecanoyl-[ACP]

  GENERIC:9646

  Is ROOT: no
  ROOT compound: GENERIC:9620

  Number of residues: 1

  O-(S-3R-hydroxytetradecanoylpantetheine-4ʼ-phosphoryl)-L-serine residue O-(S-3R-hydroxytetradecanoylpantetheine-4'-phosphoryl)-L-serine residue Name origin: UniProt - CHECKED (C) CHEBI:78474 Formula: C28H51N3O10PS Charge: -1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine

  UDP-3-O-[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine

  Name origin: UniProt - CHECKED (C)

  CHEBI:71573

  Formula: C29H50N3O18P2
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  =

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  holo-[ACP]

  holo-[ACP]

  GENERIC:9685

  Is ROOT: no
  ROOT compound: GENERIC:9620

  Number of residues: 1

  O-(pantetheine-4ʼ-phosphoryl)-L-serine residue O-(pantetheine-4'-phosphoryl)-L-serine residue Name origin: UniProt - CHECKED (C) CHEBI:64479 Formula: C14H25N3O8PS Charge: -1 Position: undefined ChEBI compound status: CHECKED (C)

  +

  UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-α-D-glucosamine

  UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine

  Name origin: UniProt - CHECKED (C)

  CHEBI:78847

  Formula: C43H75N3O20P2
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Comments:

The enzyme catalyses a step of lipid A biosynthesis. LpxD from Escherichia coli prefers (R,S)-3-hydroxytetradecanoyl-[acyl-carrier protein] over (R,S)-3-hydroxyhexadecanoyl-[acyl-carrier protein] [1]. E. coli lipid A acyltransferases do not have an absolute specificity for 14-carbon hydroxy fatty acids but can transfer fatty acids differing by one carbon unit if the fatty acid substrates are available. When grown on 1% propionic acid, lipid A also contains the odd-chain fatty acids tridecanoic acid, pentadecanoic acid, hydroxytridecanoic acid, and hydroxypentadecanoic acid [5].

Links to other databases

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]

[EC 2.3.1.191 created 2010]