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Information on EC 1.14.14.38 - valine N-monooxygenase
for references in articles please use BRENDA:EC1.14.14.38
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.38 valine N-monooxygenase
IUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
n-hydroxylating cytochrome p450, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CYP79D1
CYP79D2
EC 1.14.13.118
-
-
formerly
-
N-hydroxylating cytochrome P450
CYP79D1
-
-
-
-
CYP79D2
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2 = (E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
-
L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N-hydroxy-L-valine + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
N,N-dihydroxy-L-valine = (E)-2-methylpropanal oxime + CO2 + H2O
spontaneous
-
-
-
N-hydroxy-L-valine + [reduced NADPH-hemoprotein reductase] + O2 = N,N-dihydroxy-L-valine + [oxidized NADPH-hemoprotein reductase] + H2O
(1b)
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-valine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses two successive N-hydroxylations of L-valine, the committed step in the biosynthesis of the cyanogenic glucoside linamarin in Manihot esculenta (cassava). The product of the two hydroxylations, N,N-dihydroxy-L-valine, is labile and undergoes dehydration and decarboxylation that produce the (E) isomer of the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The enzyme can also accept L-isoleucine as substrate, with a lower activity. It is different from EC 1.14.14.39, isoleucine N-monooxygenase, which prefers L-isoleucine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Substrates: -
Products: -
Products: -
?
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
Substrates: -
Products: -
Products: -
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: -
Products: -
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: -
Products: -
?
L-isoleucine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(1E,2S)-2-methylbutanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: 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
Products: -
Products: -
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: -
Products: -
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
L-valine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: -
Products: -
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: -
Products: -
Products: -
?
L-valine + 2 [reduced NADPH-hemoprotein reductase] + 2 O2
(E)-2-methylpropanal oxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-isoleucine + O2 + NADPH + H+
(Z)-2-methylbutanal oxime + NADP+ + CO2 + H2O
Substrates: -
Products: -
Products: -
?
L-valine + O2 + NADPH + H+
(Z)-2-methylpropanal oxime + NADP+ + CO2 + H2O
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
brenda
-
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
-
brenda
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
brenda
-
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
-
brenda
preferential expression in leaf mesophyll cells positioned adjacent to the epidermis
brenda
-
preferential expression in leaf mesophyll cells positioned adjacent to the epidermis
-
brenda
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
brenda
-
in young petioles, preferential expression in the epidermis, in the two first cortex cell layers, and in the endodermis together with pericycle cells and specific parenchymatic cells around the laticifers
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
CYP79D1 and CYP79D2 are the two paralogous genes encoding the first committed enzymes in linamarin and lotaustralin synthesis. Blocking expression by RNA interference results in lines with acyanogenic leaves. Only a few of these lines are depleted with respect to cyanogenic glucoside content in tubers. Cyanogenic glucosides are synthesized in the shoot apex and transported to the root, resulting in a negative concentration gradient basipetal in the plant with the concentration of cyanogenic glucosides being highest in the shoot apex and the petiole of the first unfolded leaf
physiological function
in Lotus japonicus expressing Manihot esculenta CYP79D2, the the cyanide potential is approximately twice as high as in wild-type plants. While thelinamarin content is increased approximately 20fold, the lotaustralin content is only slightly increased. The ratio of rhodiocyanoside A and D to lotaustralin is unaltered in leaves. In roots expressing cassava CYP79D2, linamarin and lotaustralin can be detected although in much smaller quantities than in green tissue
physiological function
transgenic plants in which the expression of CYP79D1/CYP79D2 genes is selectively inhibited in leaves by antisense expression of CYP79D1/D2 gene fragments have 60-94% reduced linamarin leaf levels. These plants also have a greater than a 99% reduction in root linamarin content. Transgenic plants in which the CYP79D1/D2 transcripts are reduced to non-detectable levels in roots have normal root linamarin levels. Linamarin synthesized in leaves is transported to the roots and accounts for nearly all of the root linamarin content. Transgenic plants having reduced leaf and root linamarin content are unable to grow in the absence of NH3
physiological function
transgenic plants in which the expression of CYP79D1/D2 genes is selectively inhibited in leaves by antisense expression of CYP79D1/D2 gene fragments have 60-94% reduced linamarin leaf levels. These plants also have a greater than a 99% reduction in root linamarin content. Transgenic plants in which the CYP79D1/D2 transcripts are reduced to non-detectable levels in roots have normal root linamarin levels. Linamarin synthesized in leaves is transported to the roots and accounts for nearly all of the root linamarin content. Transgenic plants having reduced leaf and root linamarin content are unable to grow in the absence of NH3
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
physiological function
-
CYP79D1 and CYP79D2 are the two paralogous genes encoding the first committed enzymes in linamarin and lotaustralin synthesis. Blocking expression by RNA interference results in lines with acyanogenic leaves. Only a few of these lines are depleted with respect to cyanogenic glucoside content in tubers. Cyanogenic glucosides are synthesized in the shoot apex and transported to the root, resulting in a negative concentration gradient basipetal in the plant with the concentration of cyanogenic glucosides being highest in the shoot apex and the petiole of the first unfolded leaf
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). C79D1_MANES
542
1
61244
Swiss-Prot
Secretory Pathway (Reliability: 4)
C79D2_MANES
541
1
61293
Swiss-Prot
Chloroplast (Reliability: 3)
A0A396GLF8_MEDTR
146
0
16708
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycosylation of the asparagine residues at the N-terminus
glycoprotein
recombinant protein expressed in Pichia pastoris is glycosylated
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
expression of CYP79D2 from cassava in Arabidopsis thaliana results in the production of valine- and isoleucine-derived glucosinolates not normally found in this ecotype. The transgenic lines show no morphological phenotype, and the level of endogenous glucosinolates is not affected. The novel glucosinolates constitute up to 35% of the total glucosinolate content in mature rosette leaves and up to 48% in old leaves. At increased concentrations of these glucosinolates, the proportion of Val-derived glucosinolates decreases. As the isothiocyanates produced from the Val- and isoleucine-derived glucosinolates are volatile, metabolically engineered plants producing these glucosinolates have acquired novel properties with great potential for improvement of resistance to herbivorous insects and for biofumigation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
brenda
Siritunga, D.; Sayre, R.
Engineering cyanogen synthesis and turnover in cassava (Manihot esculenta)
Plant Mol. Biol.
56
661-669
2004
Manihot esculenta (Q9M7B7), Manihot esculenta (Q9M7B8)
brenda
Mikkelsen, M.D.; Halkier, B.A.
Metabolic engineering of valine- and isoleucine-derived glucosinolates in Arabidopsis expressing CYP79D2 from Cassava
Plant Physiol.
131
773-779
2003
Manihot esculenta (Q9M7B7)
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), Manihot esculenta (Q9M7B7)
brenda
Jorgensen, K.; Bak, S.; Busk, P.K.; Sorensen, C.; Olsen, C.E.; Puonti-Kaerlas, J.; Moller, B.L.
Cassava plants with a depleted cyanogenic glucoside content in leaves and tubers. Distribution of cyanogenic glucosides, their site of synthesis and transport, and blockage of the biosynthesis by RNA interference technology
Plant Physiol.
139
363-374
2005
Manihot esculenta (Q9M7B7), Manihot esculenta (Q9M7B8), Manihot esculenta MCol22 (Q9M7B7), Manihot esculenta MCol22 (Q9M7B8)
brenda
Kannangara, R.; Motawia, M.S.; Hansen, N.K.; Paquette, S.M.; Olsen, C.E.; Moller, B.L.; Jorgensen, K.
Characterization and expression profile of two UDP-glucosyltransferases, UGT85K4 and UGT85K5, catalyzing the last step in cyanogenic glucoside biosynthesis in cassava
Plant J.
68
287-301
2011
Manihot esculenta (Q9M7B7), Manihot esculenta (Q9M7B8)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.38)
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Release 2023.1 (January 2023)
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