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Entry
EC 1.14.11.39               Enzyme                                 

Name
L-asparagine hydroxylase;
L-asparagine 3-hydroxylase;
AsnO
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
BRITE hierarchy
Sysname
L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2 [RN:R10446]
Reaction(KEGG)
Substrate
L-asparagine [CPD:C00152];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
(2S,3S)-3-hydroxyasparagine [CPD:C20631];
succinate [CPD:C00042];
CO2 [CPD:C00011]
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.
History
EC 1.14.11.39 created 2013
Orthology
K18058  
L-asparagine oxygenase
Genes
SCO: 
SCO2693(SCC61A.14) SCO3236(SCE29.05c)
SCB: 
SVL: 
SCT: 
SCY: 
SHY: 
SHO: 
STRP: 
SCI: 
SLV: 
SLIV_21510(asnO1) SLIV_24200(asnO2)
SEN: 
AOI: 
ACTN: 
CAI: 
 » show all
Taxonomy
Reference
1  [PMID:17373765]
  Authors
Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA
  Title
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide.
  Journal
ACS. Chem. Biol. 2 (2007) 187-96.
  Sequence
[sco:SCO3236]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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