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BKMS-react is an integrated and non-redundant biochemical reaction database containing known enzyme-catalyzed and spontaneous reactions. Biochemical reactions collected from BRENDA, KEGG, MetaCyc and SABIO-RK were matched and integrated by aligning substrates and products.
 

:= BRENDA, := KEGG, := MetaCyc, := SABIO-RK
:= amino acid sequences := show the reaction diagram
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  • EC Number
  • Reaction
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EC Number
Reaction
Pathways
Reaction IDs
Stoichiometry Check  
Commentary
SPONTANEOUS
N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O
-
: the last step of three-step reaction (see R09403, R10027+R10028+R10029)
: A heme-thiolate protein (P-450). This enzyme catalyses 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 catalysed 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 activity. It is different from |FRAME: 1.14.13.118-RXN EC 1.14.13.118"| (valine N-monooxygenase), which prefers L-valine.
valine N-monooxygenase
N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O
-
: the last step of three-step reaction (see R09403, R10027+R10028+R10029)
: A heme-thiolate protein (P-450). This enzyme catalyses 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 catalysed 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 activity. It is different from |FRAME: 1.14.13.118-RXN EC 1.14.13.118"| (valine N-monooxygenase), which prefers L-valine.
isoleucine N-monooxygenase
N,N-dihydroxy-L-isoleucine = (1E,2S)-2-methylbutanal oxime + CO2 + H2O
-
: the last step of three-step reaction (see R09403, R10027+R10028+R10029)
: A heme-thiolate protein (P-450). This enzyme catalyses 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 catalysed 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 activity. It is different from |FRAME: 1.14.13.118-RXN EC 1.14.13.118"| (valine N-monooxygenase), which prefers L-valine.