The Enzyme Database

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Accepted name: L-asparagine hydroxylase
Reaction: L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2
Other name(s): L-asparagine 3-hydroxylase; AsnO
Systematic name: L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Strieker, M., Kopp, F., Mahlert, C., Essen, L.O. and Marahiel, M.A. Mechanistic and structural basis of stereospecific Cβ-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide. ACS Chem. Biol. 2 (2007) 187–196. [DOI] [PMID: 17373765]
[EC created 2013]

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