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IUBMB CommentsThis cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-isoleucine, the committed step in the biosynthesis of the cyanogenic glucoside lotaustralin. The product of the two hydroxylations, N,N-dihydroxy-L-isoleucine, is labile and undergoes dehydration followed by decarboxylation, producing the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-valine, but with a lower activity. cf. EC 1.14.14.38, valine N-monooxygenase.
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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
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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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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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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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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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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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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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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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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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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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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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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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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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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physiological function
enzyme is part of the biosynthetic pathway leading to nitrile glucosides rhodiocyanoside A and rhodiocyanoside D as well as the cyanogenic glucosides linamarin and lotaustralin. Lotaustralin, rhodiocyanoside A, and rhodiocyanoside D are derived from the amino acid L-Ile, whereas linamarin is derived from L-Val
physiological function
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava
physiological function
bifunctional enzyme, metabolizes L-valine as well as L-isoleucine, i.e. activities of EC 1.14.14.38 and 1.14.14.39, consistent with the cooccurrence of linamarin and lotaustralin in cassava. CYP79D1 has a higher kcat value with L-valine as substrate than with L-isoleucine, which is consistent with linamarin being the major cyanogenic glucoside in cassava
physiological function
enzyme catalyzes the conversion of Val and Ile to the corresponding aldoximes in biosynthesis of cyanogenic glucosides and nitrile glucosides in Lotus japonicus. Recombinantly expressed isoforms CYP79D3 and CYP79D4 in yeast cells show 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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Andersen, M.D.; Busk, P.K.; Svendsen, I.; Moller, B.L.
Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin: Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes
J. Biol. Chem.
275
1966-1975
2000
Manihot esculenta (Q9M7B7), Manihot esculenta (Q9M7B8), Manihot esculenta
brenda
Forslund, K.; Morant, M.; Jorgensen, B.; Olsen, C.E.; Asamizu, E.; Sato, S.; Tabata, S.; Bak, S.
Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus
Plant Physiol.
135
71-84
2004
Lotus japonicus (Q6J540), Lotus japonicus (Q6J541), Lotus japonicus
brenda
1.14.14.39 isoleucine N-monooxygenase
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