ENZYME entry: EC 188.8.131.52
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|L-valine + 2 H(+) + 2 NADPH + 2 O(2) <=> (Z)-2-methylpropanal oxime + CO(2) + 3 H(2)O + 2 NADP(+)|
- This enzyme catalyzes two successive N-hydroxylations of L-valine,
the first committed steps in the biosynthesis of the cyanogenic
glucoside linamarin in the plant Manihot esculenta (cassava).
- The product of the two hydroxylations, N,N-dihydroxy-L-valine,
is extremely labile and dehydrates spontaneously.
- The dehydrated product is then subject to a decarboxylation that
produces the oxime.
- It is still not known whether the decarboxylation is spontaneous or
catalyzed by the enzyme.
- The product, (E)-2-methylpropanal oxime, undergoes a spontaneous
isomerization to the (Z) form.
- The enzyme can also accept L-isoleucine as substrate, with a lower
- It is different from EC 184.108.40.206 which prefers L-isoleucine.
|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|
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