| Entry |
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| Name |
L-asparagine hydroxylase;
L-asparagine 3-hydroxylase;
AsnO
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| Class |
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
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| Sysname |
L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
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| Reaction(IUBMB) |
L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2 [RN: R10446]
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| Reaction(KEGG) |
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| Substrate |
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| Product |
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| Comment |
Requires Fe2+. The enzyme is only able to hydroxylate free L-asparagine. It is not active toward D-asparagine. The beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone.
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| History |
EC 1.14.11.39 created 2013
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| Orthology |
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| Genes |
SCO: | | SCB: | | SVL: | | SCT: | | SCY: | | SHY: | | SHO: | | STRP: | | SCI: | | SLV: | | SEN: | | AOI: | | ACTN: | | CAI: | |
» show all
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| Reference |
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| Authors |
Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA |
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| Title |
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide. |
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| Journal |
ACS. Chem. Biol. 2 (2007) 187-96. |
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| Sequence |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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| LinkDB |
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