Valine N-monooxygenase

Valine N-monooxygenase
Identifiers
EC no.	1.14.13.118
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Valine N-monooxygenase (EC 1.14.13.118, CYP79D1, CYP79D2) is an enzyme with systematic name L-valine,NADPH:oxygen oxidoreductase (N-hydroxylating). ^{[1] [2]} This enzyme catalyses the following chemical reaction

L-valine + 2 O₂ + 2 NADPH + 2 H⁺${\displaystyle \rightleftharpoons }$ (E)-2-methylpropanal oxime + 2 NADP⁺ + CO₂ + 3 H₂O (overall reaction)

(1a) L-valine + O₂ + NADPH + H⁺${\displaystyle \rightleftharpoons }$ N-hydroxy-L-valine + NADP⁺ + H₂O

(1b) N-hydroxy-L-valine + O2 + NADPH + H⁺${\displaystyle \rightleftharpoons }$ N,N-dihydroxy-L-valine + NADP⁺ + H₂O

(1c) N,N-dihydroxy-L-valine ${\displaystyle \rightleftharpoons }$ (E)-2-methylpropanal oxime + CO₂ + H₂O (spontaneous reaction)

Valine N-monooxygenase is a heme-thiolate protein (P-450).

References

1. Andersen MD, Busk PK, Svendsen I, Møller BL (January 2000). "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". The Journal of Biological Chemistry. 275 (3): 1966–75. doi: 10.1074/jbc.275.3.1966 . PMID   10636899.
2. Forslund K, Morant M, Jørgensen B, Olsen CE, Asamizu E, Sato S, Tabata S, Bak S (May 2004). "Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus". Plant Physiology. 135 (1): 71–84. doi:10.1104/pp.103.038059. PMC   429334 . PMID   15122013.

External links

• Valine+N-monooxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)