Valine N-monooxygenase

Valine N-monooxygenase
Identifiers
EC no.1.14.14.38
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

Valine N-monooxygenase (EC 1.14.14.38, CYP79D1, CYP79D2) is an enzyme with systematic name L-valine,NADPH:oxygen oxidoreductase (N-hydroxylating).[1]This enzyme catalyses the following sequence of chemical reactions:

2D representation of the chemical structure of valine .
valine
+ 2 NADPH + 2 H+
 
 
2 O2
2 H2O
Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right
 
 
 
N,N-dihydroxy-L-valine
+ 2 NADP+
 
 
 
CO2 + H2O
Rightward reaction arrow with minor product(s) to top right
 
 
 
2D representation of the chemical structure of Q27130845.
(E)-2-methylpropanal oxime

The enzyme uses molecular oxygen and reduced nicotinamide adenine dinucleotide phosphate (NADPH) to convert L-valine first to its N-hydroxy derivative and then to N,N-dihydroxy-L-valine. This compound is unstable and loses carbon dioxide and water to give the (E) isomer of 2-methylpropanal oxime.[2]

Valine N-monooxygenase is a cytochrome P450 protein containing heme.[3] The product oxime is an intermediate in the biosynthesis of linamarin in Lotus japonicus.[2]

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. 1 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.
  3. ↑ Enzyme 1.14.14.38 at KEGG Pathway Database.
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