The Enzyme Database

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EC 1.14.13.248     
Accepted name: L-aspartate N-monooxygenase (nitrosuccinate-forming)
Reaction: L-aspartate + 3 NADPH + 3 H+ + 3 O2 = (2S)- 2-nitrobutanedioate + 3 NADP+ + 4 H2O
(1a) L-aspartate + NADPH + H+ + O2 = N-hydroxy-L-aspartate + NADP+ + H2O
(1b) N-hydroxy-L-aspartate + NADPH + H+ + O2 = N,N-dihydroxy-L-aspartate + NADP+ + H2O
(1c) N,N-dihydroxy-L-aspartate = (2S)-2-nitrosobutanedioate + H2O (spontaneous)
(1d) (2S)-2-nitrosobutanedioate + NADPH + H+ + O2 = (2S)-2-nitrobutanedioate + NADP+ + H2O
Glossary: 2-nitrobutanedioate = nitrosuccinate
Other name(s): creE (gene name)
Systematic name: L-aspartate,NADPH:oxygen oxidoreductase [(2S)-2-nitrobutanedioate-forming]
Comments: The enzyme, found in some Actinobacteria, is involved in a pathway that forms nitrite, which is subsequently used to generate a diazo group in some secondary metabolites. Requires an FAD cofactor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Sugai, Y., Katsuyama, Y. and Ohnishi, Y. A nitrous acid biosynthetic pathway for diazo group formation in bacteria. Nat. Chem. Biol. 12 (2016) 73–75. [DOI] [PMID: 26689788]
2.  Hagihara, R., Katsuyama, Y., Sugai, Y., Onaka, H. and Ohnishi, Y. Novel desferrioxamine derivatives synthesized using the secondary metabolism-specific nitrous acid biosynthetic pathway in Streptomyces davawensis. J. Antibiot. (Tokyo) 71 (2018) 911–919. [DOI] [PMID: 30120394]
[EC 1.14.13.248 created 2021]
 
 


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