1.14.14.38: valine N-monooxygenase

This is an abbreviated version!
For detailed information about valine N-monooxygenase, go to the full flat file.

Reaction

+ 2 [reduced NADPH-hemoprotein reductase] + 2 O2 =

+ 2 [oxidized NADPH-hemoprotein reductase] +

+ 3 H2O

Synonyms

CYP79D1, CYP79D2, CYP79D3, CYP79D4, EC 1.14.13.118, N-hydroxylating cytochrome P450, valine N-monooxygenase

ECTree

1 Oxidoreductases

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.14.38 valine N-monooxygenase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
5	AA Sequence
1	Application
4	Cloned(Commentary)
8	General Information
1	Inhibitors
4	kcat/KM [mM/s]
4	KM Value [mM]
2	Localization
2	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
14	Organism
4	Pathway
1	pH Optimum
2	Posttranslational Modification
1	Protein Variants
1	Purification (Commentary)
4	Reaction
12	Reference
13	Source Tissue
15	Substrates and Products (Substrate)
2	Subunits
13	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
5	Turnover Number [1/s]

Systematic Name

print visible entries

print all entries

Systematic Name on EC 1.14.14.38 - valine N-monooxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Systematic Name Search

L-valine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)

A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.