ENZYME entry: EC 126.96.36.199
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|L-valine + 2 O(2) + 2 [reduced NADPH--hemoprotein reductase] <=> (E)-2-methylpropanal oxime + 2 [oxidized NADPH--hemoprotein reductase] + CO(2) + 3 H(2)O|
- 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 188.8.131.52.
- Formerly EC 184.108.40.206.
|PRIAM enzyme-specific profiles||220.127.116.11|
|KEGG Ligand Database for Enzyme Nomenclature||18.104.22.168|
|IUBMB Enzyme Nomenclature||22.214.171.124|
|MEDLINE||Find literature relating to 126.96.36.199|
|Rhea expert-curated reactions||188.8.131.52|
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.-.-.-