1.14.14.38: valine N-monooxygenase
This is an abbreviated version!
For detailed information about valine N-monooxygenase, go to the full flat file.
Reaction
+ 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = + 2 [oxidized NADPH-hemoprotein reductase] + + 3 H2O
Synonyms
CYP79D1, CYP79D2, CYP79D3, CYP79D4, EC 1.14.13.118, N-hydroxylating cytochrome P450, valine N-monooxygenase
ECTree
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Substrates Products
Substrates Products on EC 1.14.14.38 - valine N-monooxygenase
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REACTION DIAGRAM
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
L-isoleucine + O2 + NADPH + H+
(Z)-2-methylbutanal oxime + NADP+ + CO2 + H2O
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L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
L-valine + O2 + NADPH + H+
(Z)-2-methylpropanal oxime + NADP+ + CO2 + H2O
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(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
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(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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overall reaction
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L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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overall reaction
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?
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
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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
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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
under saturating substrate conditions CYP79D1 has a higher conversion rate using L-valine as substrate. The conversion rate of L-isoleucine is approximately 60% of that observed for L-valine, consistent with higher accumulation of linamarin compared with lotaustralin in vivo in cassava
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enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39, 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-isoleucine, reaction of EC 1.14.14.39, 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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no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
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additional information
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no substrate: L-leucine, L-phenylalanine, L-tyrosine. The observed substrate specificity corresponds with the in vivo presence of only L-valine- and L-isoleucine-derived cyanogenic glucosides in cassava
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additional information
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enzyme additionally acts on L-isoleucine, reaction of EC 1.14.14.39. 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-isoleucine, reaction of EC 1.14.14.39. 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. 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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