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Information on EC 1.14.14.37 - 4-hydroxyphenylacetaldehyde oxime monooxygenase
for references in articles please use BRENDA:EC1.14.14.37
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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
1.14.14.37 4-hydroxyphenylacetaldehyde oxime monooxygenase
IUBMB Comments
This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
The enzyme appears in viruses and cellular organisms
- 1.14.14.37
- heme
- fmn
- cyp1a2
-
nadh-cytochrome
- 7-ethoxyresorufin
-
p450-dependent
- 7-ethoxycoumarin
-
nadph-p450
-
o-deethylase
-
one-electron
-
alpha-hydroxylase
-
o-deethylation
- dt-diaphorase
-
drug-metabolizing
- benzphetamine
- biliverdin
- cyp2b4
- dhurrin
-
alpha-hydroxylation
-
1.6.2.4
-
p450-mediated
-
cdna-expressed
-
o-dealkylation
-
fmn-binding
-
p450-catalyzed
- dilauroylphosphatidylcholine
- agriculture
- biotechnology
- analysis
Reaction Schemes
showSynonyms
nadph-cytochrome p450 reductase, cyp71e1, cyp71e, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxybenzeneacetaldehyde oxime monooxygenase
-
-
-
-
4-hydroxyphenylacetaldehyde oxime monooxygenase
-
-
-
-
CYP71E1
cytochrome P450II-dependent monooxygenase
-
-
-
-
EC 1.14.13.42
-
-
formerly
-
EC 1.14.13.68
-
-
formerly
-
NADPH-cytochrome P450 reductase
-
-
-
-
CYP71E1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
overall reaction
-
-
-
(E)-4-hydroxyphenylacetaldehyde oxime = (Z)-4-hydroxyphenylacetaldehyde oxime
(1a)
-
-
-
(Z)-4-hydroxyphenylacetaldehyde oxime = 4-hydroxyphenylacetonitrile + H2O
(1b)
-
-
-
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
(1c)
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
(E)-4-hydroxyphenylacetaldehyde oxime,[reduced NADPHĀhemoprotein reductase]:oxygen oxidoreductase
This cytochrome P-450 (heme thiolate) enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum. It catalyses three different activities - isomerization of the (E) isomer to the (Z) isomer, dehydration, and C-hydroxylation.
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CAS REGISTRY NUMBER
COMMENTARY
213017-82-4
-
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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
(E)-4-Hydroxyphenylacetaldehyde oxime
(Z)-4-Hydroxyphenylacetaldehyde oxime
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(E)-phenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-mandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: oxime dervied from phenylalanine, 35% of the activity with (E)-4-hydroxyphenylacetaldehyde oxime
Products: -
Products: -
?
(Z)-3-methylbutanaloxime + [reduced NADPH-hemoprotein reductase] + O2
2-hydroxy-3-methylbutyronitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: -
Products: -
?
(Z)-4-hydroxyphenylacetaldehyde oxime
4-hydroxyphenylacetonitrile + H2O
Substrates: -
Products: -
Products: -
?
2-hydroxy(p-hydroxyphenyl)acetaldoxime
4-hydroxymandelonitrile + H2O
-
Substrates: poor substrate
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: overall reaction
Products: overall reaction
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: -
Products: overall reaction. NADPH is a much better cofactor for NADPH-hemoprotein reductase than NADH although NADH does support the entire catalytic cycle
Products: overall reaction. NADPH is a much better cofactor for NADPH-hemoprotein reductase than NADH although NADH does support the entire catalytic cycle
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: involved in dhurrin synthesis
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
-
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: CYP71E1 metabolizes aromatic oximes efficiently, whereas aliphatic oximes are slowly metabolized
Products: -
Products: -
?
additional information
?
-
-
Substrates: CYP71E1 metabolizes aromatic oximes efficiently, whereas aliphatic oximes are slowly metabolized
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
(E)-4-Hydroxyphenylacetaldehyde oxime
(Z)-4-Hydroxyphenylacetaldehyde oxime
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
(Z)-3-methylbutanaloxime + [reduced NADPH-hemoprotein reductase] + O2
2-hydroxy-3-methylbutyronitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: -
Products: -
?
(Z)-4-hydroxyphenylacetaldehyde oxime
4-hydroxyphenylacetonitrile + H2O
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylacetonitrile + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + H2O
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
-
Substrates: -
Products: -
Products: -
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2
(S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O
Substrates: involved in dhurrin synthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
NADPH-Cytochrome P450 Reductase Mediates the Resistance of Aphis (Toxoptera) citricidus (Kirkaldy) to Abamectin.
Adenoma
High expression of cytochrome b5 in adrenocortical adenomas from patients with Cushing's syndrome associated with high secretion of adrenal androgens.
Adrenal Hyperplasia, Congenital
Human cytochrome P450 oxidoreductase deficiency caused by the Y181D mutation: molecular consequences and rescue of defect.
Adrenocortical Adenoma
High expression of cytochrome b5 in adrenocortical adenomas from patients with Cushing's syndrome associated with high secretion of adrenal androgens.
Breast Neoplasms
Epitope characterization of an aromatase monoclonal antibody suitable for the assessment of intratumoral aromatase activity.
Breast Neoplasms
Human NADPH-cytochrome p450 reductase overexpression does not enhance the aerobic cytotoxicity of doxorubicin in human breast cancer cell lines.
Carcinogenesis
The levels of quinone reductases, superoxide dismutase and glutathione-related enzymatic activities in diethylstilbestrol-induced carcinogenesis in the kidney of male Syrian golden hamsters.
Carcinoma, Hepatocellular
Relationship between cytochrome P450 catalytic cycling and stability: fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH-cytochrome P450 reductase.
Carcinoma, Hepatocellular
The effect of dimethyl sulfoxide on the function of cytochrome P450 2D6 in HepG2 cells upon the co-expression with NADPH-cytochrome P450 reductase.
Cardiotoxicity
Deletion of the NADPH-cytochrome P450 reductase gene in cardiomyocytes does not protect mice against doxorubicin-mediated acute cardiac toxicity.
Cushing Syndrome
High expression of cytochrome b5 in adrenocortical adenomas from patients with Cushing's syndrome associated with high secretion of adrenal androgens.
Dehydration
Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L.) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin.
Dehydration
Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
Dehydration
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.
Drug-Related Side Effects and Adverse Reactions
In vivo mechanisms of tissue-selective drug toxicity: effects of liver-specific knockout of the NADPH-cytochrome P450 reductase gene on acetaminophen toxicity in kidney, lung, and nasal mucosa.
Endotoxemia
Microsomal Ethanol-Oxidizing System: Success Over 50 Years and an Encouraging Future.
Fatty Liver
Hepatic gene expression changes in mouse models with liver-specific deletion or global suppression of the NADPH-cytochrome P450 reductase gene. Mechanistic implications for the regulation of microsomal cytochrome P450 and the fatty liver phenotype.
Gynecomastia
Studies on the interactions between drugs and estrogen: analytical method for prediction system of gynecomastia induced by drugs on the inhibitory metabolism of estradiol using Escherichia coli coexpressing human CYP3A4 with human NADPH-cytochrome P450 reductase.
Herpes Zoster
The primate adrenal zona reticularis is defined by expression of cytochrome b5, 17alpha-hydroxylase/17,20-lyase cytochrome P450 (P450c17) and NADPH-cytochrome P450 reductase (reductase) but not 3beta-hydroxysteroid dehydrogenase/delta5-4 isomerase (3beta-HSD).
Hypersensitivity
Proximal Tubular Vacuolization and Hypersensitivity to Drug-Induced Nephrotoxicity in Male Mice With Decreased Expression of the NADPH-Cytochrome P450 Reductase.
Hyperthyroidism
Liver microsomal parameters related to oxidative stress and antioxidant systems in hyperthyroid rats subjected to acute lindane treatment.
Leukemia, Myeloid, Acute
NADPH-Cytochrome P450 Reductase Is Regulated by All-Trans Retinoic Acid and by 1,25-Dihydroxyvitamin D3 in Human Acute Myeloid Leukemia Cells.
Mycoses
Haplotype Diversity of NADPH-Cytochrome P450 Reductase Gene of Ophiocordyceps sinensis and the Effect on Fungal Infection in Host Insects.
Neoplasms
Alterations in expression of CYP1A1 and NADPH-cytochrome P450 reductase during lung tumor development in SWR/J mice.
Neoplasms
Aryl hydrocarbon hydroxylase activity in chemically induced and toremifene-treated mammary tumors in rats.
Neoplasms
Retention mechanism of hypoxia selective nuclear imaging/radiotherapeutic agent cu-diacetyl-bis(N4-methylthiosemicarbazone) (Cu-ATSM) in tumor cells.
Reperfusion Injury
Inhibition of NADPH-cytochrome P450 reductase by tannic acid in rat liver microsomes and primary hepatocytes: Methodological artifacts and application to ischemia-reperfusion injury.
Schistosomiasis
Hepatic cytochrome P450s, phase II enzymes and nuclear receptors are downregulated in a Th2 environment during Schistosoma mansoni infection.
steroid 21-monooxygenase deficiency
Human cytochrome P450 oxidoreductase deficiency caused by the Y181D mutation: molecular consequences and rescue of defect.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8.4
-
formation of p-hydroxybenzaldehyde from L-tyrosine in microsomal fractions
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
brenda
the site of dhurrin synthesis shifts from leaves to stem during plant development. At all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes
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
-
a microsomal fraction from seedlings of Sorghum bicolor catalyzes the conversion of L-tyrosine to 4-hydroxymandelonitrile via 4-hydroxyphenylacetaldoxime
physiological function
at all stages, the content of dhurrin correlates well with the activity of the two biosynthetic enzymes, CYP79A1 and CYP71E1, and with the protein and mRNA level for the two enzymes. During development, the activity of tyrosine N-monooxygenase CYP79A1 is lower than the activity of 4-hydroxyphenylacetaldehyde oxime monooxygenase CYP71E1, suggesting that CYP79A1 catalyzes the rate-limiting step in dhurrin synthesis
physiological function
-
during biosynthesis of dhurrin, 4-hydroxyphenylacetonitrile functions as an intermediate, and not 2-hydroxy(4-hydroxyphenyl)-acetaldoxime
physiological function
full length CYP79A1, CYP71E1 and NADPH P450 oxidoreductase of the dhurrin pathway are reconstituted individually in nanoscale lipid patches, nanodiscs, and directly immobilized on unmodified gold electrodes. Cyclic voltammograms of CYP79A1 and CYP71E1 reveal reversible redox peaks with average midpoint potentials of 80 mV and 72 mV vs. Ag/AgCl, respectively. NADPH P450 oxidoreductase yields two pairs of redox peaks with midpoint potentials of 90 mV and -300 mV, respectively. The average heterogeneous electron transfer rate constant is calculated to be 1.5 per s
physiological function
the biosynthetic pathway for the cyanogenic glucoside dhurrin in Sorghum involves the sequential production of (E)- and (Z)-4-hydroxyphenylacetaldoxime. Monooxygenae CYP79A1 catalyzes conversion of tyrosine to (E)-4-hydroxyphenylacetaldoxime, whereas monooxygenase CYP71E1 catalyzes conversion of (E)-4-hydroxyphenylacetaldoxime into the corresponding geometrical Z-isomer as required for its dehydration into a nitrile, the next intermediate in cyanogenic glucoside synthesis
physiological function
the enzyme is a multifunctional P450 catalyzing dehydration of (Z)-4-hydroxyphenylacetaldoxime to 4-hydroxyphenylacetonitrile and C-hydroxylation of 4-hydroxyphenylacetonitrile during biosynthesis of the cyanogenic glucoside beta-D-glucopyranosyloxy-(S)-4-hydroxymandelonitrile (dhurrin)
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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). C71E1_SORBI
531
2
59088
Swiss-Prot
Mitochondrion (Reliability: 5)
B9T872_RICCO
207
0
23768
TrEMBL
other Location (Reliability: 5)
B9R857_RICCO
497
0
56756
TrEMBL
Secretory Pathway (Reliability: 5)
B9SVN7_RICCO
507
2
57778
TrEMBL
Secretory Pathway (Reliability: 3)
B9SY53_RICCO
438
1
50634
TrEMBL
Secretory Pathway (Reliability: 1)
B9RM57_RICCO
504
1
57687
TrEMBL
Secretory Pathway (Reliability: 3)
B9RHX3_RICCO
533
0
59582
TrEMBL
Chloroplast (Reliability: 3)
B9RAR9_RICCO
508
1
57278
TrEMBL
Secretory Pathway (Reliability: 3)
B9RMU6_RICCO
208
0
23602
TrEMBL
other Location (Reliability: 4)
B9RAS3_RICCO
521
1
58842
TrEMBL
Secretory Pathway (Reliability: 1)
B9RHW8_RICCO
523
1
58692
TrEMBL
Secretory Pathway (Reliability: 2)
B9S9Q2_RICCO
499
0
56727
TrEMBL
Secretory Pathway (Reliability: 3)
B9SVN6_RICCO
112
0
12819
TrEMBL
other Location (Reliability: 3)
A0A2P6P3M1_ROSCH
209
0
24020
TrEMBL
other Location (Reliability: 3)
B9RHX0_RICCO
497
1
55854
TrEMBL
Secretory Pathway (Reliability: 2)
B9RHW6_RICCO
534
0
59918
TrEMBL
Chloroplast (Reliability: 3)
A0A2P6QXL6_ROSCH
493
1
56058
TrEMBL
Secretory Pathway (Reliability: 1)
A0A2P6R116_ROSCH
66
0
7439
TrEMBL
other Location (Reliability: 4)
A0A0B2RR52_GLYSO
155
0
17886
TrEMBL
other Location (Reliability: 5)
B9TA51_RICCO
267
0
30457
TrEMBL
other Location (Reliability: 4)
B9S3I3_RICCO
315
0
35246
TrEMBL
other Location (Reliability: 4)
B9SB70_RICCO
78
1
8702
TrEMBL
Mitochondrion (Reliability: 3)
B9SB66_RICCO
509
2
58303
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6QXL0_ROSCH
513
1
58637
TrEMBL
Secretory Pathway (Reliability: 1)
B9SA81_RICCO
221
0
25198
TrEMBL
other Location (Reliability: 3)
B9S9U3_RICCO
507
1
58001
TrEMBL
Secretory Pathway (Reliability: 2)
B9T870_RICCO
208
0
23569
TrEMBL
other Location (Reliability: 2)
B9RAS2_RICCO
508
1
57494
TrEMBL
Secretory Pathway (Reliability: 2)
B9RHW4_RICCO
501
1
56765
TrEMBL
Secretory Pathway (Reliability: 2)
B9T234_RICCO
500
1
56595
TrEMBL
Secretory Pathway (Reliability: 1)
B9T0U6_RICCO
518
1
59265
TrEMBL
other Location (Reliability: 5)
B9RHX6_RICCO
473
0
53038
TrEMBL
Chloroplast (Reliability: 5)
B9TJ16_RICCO
220
0
25341
TrEMBL
other Location (Reliability: 4)
B9T233_RICCO
500
1
56748
TrEMBL
Secretory Pathway (Reliability: 3)
B9RAS4_RICCO
527
1
59802
TrEMBL
Secretory Pathway (Reliability: 5)
B9RAS1_RICCO
295
0
34141
TrEMBL
other Location (Reliability: 3)
B9SB69_RICCO
509
2
58095
TrEMBL
Secretory Pathway (Reliability: 5)
A0A084GEV4_PSEDA
544
0
61784
TrEMBL
Secretory Pathway (Reliability: 4)
B9S895_RICCO
304
1
35099
TrEMBL
Secretory Pathway (Reliability: 3)
B9RMP3_RICCO
520
1
59110
TrEMBL
Secretory Pathway (Reliability: 1)
B9SA84_RICCO
532
0
59845
TrEMBL
Chloroplast (Reliability: 4)
A0A2P6R100_ROSCH
512
2
58012
TrEMBL
Mitochondrion (Reliability: 5)
B9SB73_RICCO
499
2
57365
TrEMBL
Secretory Pathway (Reliability: 3)
B9RM58_RICCO
524
1
59607
TrEMBL
Secretory Pathway (Reliability: 2)
B9SBU8_RICCO
507
1
57356
TrEMBL
Secretory Pathway (Reliability: 2)
B9RAR8_RICCO
510
1
57963
TrEMBL
Secretory Pathway (Reliability: 3)
B9RCY8_RICCO
441
1
50453
TrEMBL
Secretory Pathway (Reliability: 1)
B9TPU9_RICCO
268
1
30510
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6QXJ9_ROSCH
513
1
58555
TrEMBL
Secretory Pathway (Reliability: 1)
B9T235_RICCO
504
1
57123
TrEMBL
Secretory Pathway (Reliability: 2)
B9SJ86_RICCO
362
2
41197
TrEMBL
Secretory Pathway (Reliability: 5)
B9SVN9_RICCO
504
0
57683
TrEMBL
Secretory Pathway (Reliability: 2)
B9SB72_RICCO
480
2
54608
TrEMBL
Mitochondrion (Reliability: 5)
A0A2P6QXL5_ROSCH
498
1
56956
TrEMBL
Secretory Pathway (Reliability: 1)
A0A072UEP4_MEDTR
116
1
13042
TrEMBL
Secretory Pathway (Reliability: 1)
B9R855_RICCO
496
0
56874
TrEMBL
Secretory Pathway (Reliability: 4)
A0A2P6P3M5_ROSCH
70
1
7657
TrEMBL
Secretory Pathway (Reliability: 3)
B9RHW2_RICCO
506
1
56766
TrEMBL
Secretory Pathway (Reliability: 2)
B9SVN8_RICCO
512
2
58696
TrEMBL
Secretory Pathway (Reliability: 4)
A0A0B2NPM1_GLYSO
126
1
14030
TrEMBL
Secretory Pathway (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
CYP71E1 is labile and prone to rapid denaturation at room temperature. CYP71E1 is isolated in the low spin form.
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution with NADPH-P450 oxidoreductase in micelles of L-alpha-dilauroyl phosphatidylcholine
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
direct electrochemical investigation of plant cytochrome P450s by nanodisc technology. Full length CYP79A1, CYP71E1 and NADPH P450 oxidoreductase of the dhurrin pathway are reconstituted individually in nanoscale lipid patches, nanodiscs, and directly immobilized on unmodified gold electrodes. Cyclic voltammograms of CYP79A1 and CYP71E1 reveal reversible redox peaks with average midpoint potentials of 80 mV and 72 mV vs. Ag/AgCl, respectively. NADPH P450 oxidoreductase yields two pairs of redox peaks with midpoint potentials of 90 mV and -300 mV, respectively. The average heterogeneous electron transfer rate constant is calculated to be 1.5 per s
biotechnology
agriculture
simultaneous expression of the two multifunctional sorghum cytochrome P450 enzymes CYP79A1 and CYP71E1 in tobacco and Arabidopsis leads to cyanogenic plants. In transgenic plants expressing CYP79A1 as well as CYP71E1, the activity of CYP79A1 is higher than that of CYP71E1, resulting in the accumulation of several 4-hydroxyphenylacetaldoxime-derived products in the addition to those derived from 4-hydroxymandelonitrile. In transgenic Arabidopsis expressing CYP71E1, this enzyme and the enzymes of the pre-existing glucosinolate pathway compete for the 4-hydroxyphenylacetaldoxime as substrate, resulting in the formation of small amounts of 4-hydroxybenzylglucosinolate
agriculture
transgenic Arabidopsis thaliana plants expressing CYP79A1, CYP71E1, and UGT85B1 from Sorghum bicolor, i.e. the entire biosynthetic pathway for the tyrosine-derived cyanogenic glucoside dhurrin, accumulate 4% dry-weight dhurrin with marginal inadvertent effects on plant morphology, free amino acid pools, transcriptome, and metabolome. Plants expressing only CYP79A1 accumulate 3% dry weight of the tyrosine-derived glucosinolate, 4-hydroxybenzylglucosinolate with no morphological pleitropic effects. Insertion of CYP79A1 plus CYP71E1 results in stunted plants, transcriptome alterations, accumulation of numerous glucosides derived from detoxification of intermediates in the dhurrin pathway, and in loss of the brassicaceae-specific UV protectants sinapoyl glucose and sinapoyl malate and kaempferol glucosides. The accumulation of glucosides in the plants expressing CYP79A1 and CYP71E1 is not accompanied by induction of glycosyltransferases
biotechnology
engineering of the dhurrin pathway from Sorghum bicolor into the chloroplasts of Nicotiana tabacum. The entire pathway can be introduced into the chloroplast by integrating membrane-bound cytochrome P450 enzymes CYP79A1, CYP71E1, and soluble glucosyltransferase UGT85B1 into a neutral site of the Nicotiana tabacum chloroplast genome. The two P450s and the UGT85B1 are functional when expressed in the chloroplasts and convert endogenous tyrosine into dhurrin using electrons derived directly from the photosynthetic electron transport chain, without the need for the presence of an NADPH-dependent P450 oxidoreductase. The dhurrin produced in the engineered plants amounts to 0.1-0.2% of leaf dry weight compared to 6% in sorghum
biotechnology
in vitro reconstitution of the entire dhurrin biosynthetic pathway from tyrosine is accomplished by the insertion of CYP79 (tyrosine N-hydroxylase), P450ox, and NADPH-P450 oxidoreductase in lipid micelles in the presence of uridine diphosphate glucose glucosyltransferase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McFarlane, I.J.; Lees, E.M
Conn, E.E.: The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor
J. Biol. Chem.
250
4708-4713
1975
Sorghum bicolor
brenda
Shimada, M.; Conn, E.E.
The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile
Arch. Biochem. Biophys.
180
199-207
1977
Sorghum bicolor
brenda
Bak, S.; Kahn, R.A.; Nielsen, H.L.; Moeller, B.L.; Halkier, B.A.
Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L:) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin
Plant Mol. Biol.
36
393-405
1998
Sorghum bicolor
brenda
Kahn, R.A.; Fahrendorf, T.; Halkier, B.A.; Moller, B.L.
Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
Arch. Biochem. Biophys.
363
9-18
1999
Sorghum bicolor (O48958), Sorghum bicolor
brenda
Nielsen, K.A.; Olsen, C.E.; Pontoppidan, K.; Moller, B.L.
Leucine-derived cyano glucosides in barley
Plant Physiol.
129
1066-1075
2002
Hordeum vulgare
brenda
Busk, P.K.; Moller, B.L.
Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants
Plant Physiol.
129
1222-1231
2002
Sorghum bicolor, Sorghum bicolor (O48958)
brenda
Kristensen, C.; Morant, M.; Olsen, C.E.; Ekstrom, C.T.; Galbraith, D.W.; Moller, B.L.; Bak, S.
Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome
Proc. Natl. Acad. Sci. USA
102
1779-1784
2005
Sorghum bicolor (O48958), Sorghum bicolor
brenda
Jensen, K.; Osmani, S.A.; Hamann, T.; Naur, P.; Moller, B.L.
Homology modeling of the three membrane proteins of the dhurrin metabolon: catalytic sites, membrane surface association and protein-protein interactions
Phytochemistry
72
2113-2123
2011
Sorghum bicolor
brenda
Gnanasekaran, T.; Karcher, D.; Nielsen, A.Z.; Martens, H.J.; Ruf, S.; Kroop, X.; Olsen, C.E.; Motawie, M.S.; Pribil, M.; M?ller, B.L.; Bock, R.; Jensen, P.E.
Transfer of the cytochrome P450-dependent dhurrin pathway from Sorghum bicolor into Nicotiana tabacum chloroplasts for light-driven synthesis
J. Exp. Bot.
67
2495-2506
2016
Sorghum bicolor (O48958)
brenda
Clausen, M.; Kannangara, R.M.; Olsen, C.E.; Blomstedt, C.K.; Gleadow, R.M.; Jorgensen, K.; Bak, S.; Motawie, M.S.; Moller, B.L.
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways
Plant J.
84
558-573
2015
Sorghum bicolor (O48958)
brenda
Kahn, R.A.; Bak, S.; Svendsen, I.; Halkier, B.A.; Moller, B.L.
Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum
Plant Physiol.
115
1661-1670
1997
Sorghum bicolor (O48958)
brenda
Bak, S.; Olsen, C.E.; Halkier, B.A.; Moller, B.L.
Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in Dhurrin biosynthesis
Plant Physiol.
123
1437-1448
2000
Sorghum bicolor (O48958)
brenda
Bavishi, K.; Laursen, T.; Martinez, K.; Moller, B.; Della Pia, E.
Application of nanodisc technology for direct electrochemical investigation of plant cytochrome P450s and their NADPH P450 oxidoreductase
Sci. Rep.
6
29459
2016
Sorghum bicolor (O48958), Sorghum bicolor
brenda
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