EC 1.14.14.39 - Isoleucine N-monooxygenase

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IntEnz Enzyme Nomenclature
EC 1.14.14.39

Names

Accepted name:
isoleucine N-monooxygenase
Other names:
CYP79D3
CYP79D4
Systematic name:
L-isoleucine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)

Reaction

Cofactor

Comments:

This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-valine, but with a lower activity. cf. EC 1.14.14.38, valine N-monooxygenase. Formerly EC 1.4.13.117.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0102001
UniProtKB/Swiss-Prot:

References

  1. Andersen, M. D., Busk, P. K., Svendsen, I., Møller, B. L.
    Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes.
    J. Biol. Chem. 275: 1966-1975 (2000). [PMID: 10636899]
  2. Forslund, K., Morant, M., Jørgensen, B., Olsen, C. E., Asamizu, E., Sato, S., Tabata, S., Bak, S.
    Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus.
    Plant Physiol. 135: 71-84 (2004). [PMID: 15122013]

[EC 1.14.14.39 created 2010 as EC 1.14.13.117, transferred 2017 to EC 1.14.14.39]