ENZYME entry: EC 184.108.40.206
View entry in original ENZYME format
View entry in raw text format (no links)
in this entry
|L-isoleucine + 2 H(+) + 2 NADPH + 2 O(2) <=> (E)-2-methylbutanal oxime + CO(2) + 3 H(2)O + 2 NADP(+)|
- This enzyme catalyzes two successive N-hydroxylations of
L-isoleucine, the first committed steps in the biosynthesis of the
cyanogenic glucoside lotaustralin in the plant Lotus japonicus.
- The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine,
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-methylbutanal oxime, undergoes a spontaneous
isomerization to the (Z) form.
- The enzyme can also accept L-valine as substrate, with a lower
- It is different from EC 220.127.116.11 which prefers L-valine.
|PRIAM enzyme-specific profiles||18.104.22.168|
|KEGG Ligand Database for Enzyme Nomenclature||22.214.171.124|
|IUBMB Enzyme Nomenclature||126.96.36.199|
|MEDLINE||Find literature relating to 188.8.131.52|
, with possibility to download in different formats, align etc.
entries corresponding to 1.14.13.-
entries corresponding to 1.14.-.-
entries corresponding to 1.-.-.-