1.14.14.39: isoleucine N-monooxygenase
This is an abbreviated version!
For detailed information about isoleucine N-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.39
Reaction
Synonyms
CYP79D1, CYP79D2, CYP79D3, CYP79D4, EC 1.14.13.117, valine N-monooxygenase
ECTree
1.14.14.39 isoleucine N-monooxygenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.14.39 - isoleucine N-monooxygenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
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?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
higher catalytic efficiency with L-Ile as substrate than with L-Val, in agreement with lotaustralin and rhodiocyanoside A and D being the major cyanogenic and nitrile glucosides in Lotus japonicus
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?
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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overall reaction
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?
L-isoleucine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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overall reaction
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?
additional information
?
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metabolism of L-Leu, L-Phe, or L-Tyr to the corresponding oximes is not detectable in consistence with the absence of cyanogenic glucosides derived from these amino acids. No substrate: L-Trp, L-Met, L-Pro
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?
additional information
?
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metabolism of L-Leu, L-Phe, or L-Tyr to the corresponding oximes is not detectable in consistence with the absence of cyanogenic glucosides derived from these amino acids. No substrate: L-Trp, L-Met, L-Pro
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?
additional information
?
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metabolism of L-Leu, L-Phe, or L-Tyr to the corresponding oximes is not detectable in consistence with the absence of cyanogenic glucosides derived from these amino acids. No substrate: L-Trp, L-Met, L-Pro
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?
additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
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?
additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
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?
additional information
?
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38, the catalytic efficiency (Kcat/Km) being 6fold higher with L-Ile than with L-Val as substrate. No substrates: L-Tyr, L-Phe, L-Leu, L-Trp, L-Met, and L-Pro
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?
additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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?
additional information
?
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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?
additional information
?
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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?
additional information
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enzyme additionally acts on L-valine, reaction of EC 1.14.14.38. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine. No substrates: D-valine, D-isoleucine, L-leucine, L-phenylalanine, or L-tyrosine
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