ENZYME entry: EC 184.108.40.206
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|L-valine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] <=> (E)-2-methylpropanal oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase]|
- This enzyme catalyzes 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
catalyzed by the enzyme.
- The enzyme can also accept L-isoleucine as substrate, with a lower
- It is different from EC 220.127.116.11.
- Formerly EC 18.104.22.168.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|Rhea expert-curated reactions||220.127.116.11|
entries corresponding to 1.14.14.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-