| EC |
1.14.11.39 |
| 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, Gene, KEGG, MetaCyc, PDB |
| References: |
| 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] |
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| [EC 1.14.11.39 created 2013] |
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