IntEnz

EC 1.14.11.39 - L-asparagine oxygenase

IntEnz Enzyme Nomenclature
EC 1.14.11.39

Names

Reaction

• 25772 [IUBMB]
  2-oxoglutarate

  2-oxoglutarate

  Name origin: UniProt - CHECKED (C)

  CHEBI:16810

  Formula: C5H4O5
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  L-asparagine

  L-asparagine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58048

  Formula: C4H8N2O3
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  O₂

  O2

  Name origin: UniProt - CHECKED (C)

  CHEBI:15379

  Formula: O2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  (2S,3S)-3-hydroxyasparagine

  (2S,3S)-3-hydroxyasparagine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58850

  Formula: C4H8N2O4
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  CO₂

  CO2

  Name origin: UniProt - CHECKED (C)

  CHEBI:16526

  Formula: CO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  succinate

  succinate

  Name origin: UniProt - CHECKED (C)

  CHEBI:30031

  Formula: C4H4O4
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

Cofactor

• Fe²⁺

Comments:

Requires Fe2+. The enzyme is only able to hydroxylate free L-asparagine. It is not active toward D-asparagine. The β-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone.

Links to other databases

References

1. Strieker, M., Kopp, F., Mahlert, C., Essen, L. O., Marahiel, M. A.
   Mechanistic and structural basis of stereospecific Cβ-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide.
   ACS Chem. Biol. 2 : 187-196 (2007). [PMID: 17373765]

[EC 1.14.11.39 created 2013]