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Information on EC 1.14.14.36 - tyrosine N-monooxygenase
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1.14.14.36 tyrosine N-monooxygenaseIUBMB Comments
A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
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Word Map
- 1.14.14.36
- sorghum
- glucoside
- dhurrin
- bicolor
- cyp71e1
- glucosinolate
- oxime
- moench
-
nitril
- aldoximes
- p-hydroxyphenylacetaldoxime
- p-hydroxymandelonitrile
-
leucine-derived
- ugt85b1
- udp-glucosyltransferase
-
c-hydroxylation
- phenylacetaldoxime
-
tyrosine-derived
- linamarin
- n-hydroxytyrosine
- agriculture
- p-hydroxyphenylacetaldehyde
- biotechnology
- indole-3-acetaldoxime
- lotaustralin
- analysis
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
cyp79a1, cyp79, cytochrome p450tyr, cytochrome p-450tyr, p450tyr, tyrosine n-hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome P-450tyr
-
-
-
-
Cytochrome P450Tyr
EC 1.14.13.41
-
-
formerly
-
tyrosine N-hydroxylase
Tyrosine N-monooxygenase
-
-
-
-
Cytochrome P450Tyr
-
-
-
-
tyrosine N-hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
overall reaction
-
-
-
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
(1a)
-
-
-
N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
(1c)
-
-
-
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
(1b)
-
-
-
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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
L-tyrosine,[reduced NADPH-hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
A cytochrome P-450 (heme-thiolate) protein. The enzyme from Sorghum is involved in the biosynthesis of the cyanogenic glucoside dhurrin. In Sinapis alba (white mustard) the enzyme is involved in the biosynthesis of the glucosinolate sinalbin.
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CAS REGISTRY NUMBER
COMMENTARY
159447-19-5
-
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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
1-nitro-2-(4-hydroxyphenyl)ethane + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
involvement of 1-nitro-2-(4-hydroxyphenyl)ethane or more likely its aci-nitro tautomer as an intermediate between N-hydroxytyrosine and 4-hydroxyphenylacetaldehyde oxime
-
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
L-tyrosine + O2 + NADPH + H+
N-hydroxy-L-tyrosine + NADP+ + H2O
-
-
-
r
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
N,N-dihydroxy-L-tyrosine
(E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
-
-
-
?
N-hydroxy-L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [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
-
-
-
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
overall reaction
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
overall reaction. NADPH is a much better cofactor for NADPH-hemoprotein reductase than NADH although NADH does support the entire catalytic cycle
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
intermediate products: N-hydroxytyrosine, N,N-dihydroxytyrosine, (E)-p-hydroxyphenylacetaldoxime
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
overall reaction, P450Tyr is a multifunctional tyrosine N-hydroxylase catalyzing the double N-hydroxylation of L-tyrosine to N,N-dihydroxy-L-tyrosine which dehydrates and decarboxylates to 4-hydroxyphenylacetaldoxime
-
-
?
L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
high substrate specificity
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
involvement of 1-nitro-2-(4-hydroxyphenyl)ethane or more likely its aci-nitro tautomer as an intermediate between N-hydroxytyrosine and 4-hydroxyphenylacetaldehyde oxime
-
-
?
additional information
?
-
-
P450Tyr does not metabolize L-phenylalanine
-
-
?
additional information
?
-
-
CYP79A1 has a very high substrate specificity, tyrosine being the only substrate found. Analogs 1-nitro-2-p-(hydroxyphenyl)ethane, N-hydroxytyrosine and phenylalanine are able to bind to the enzyme, without being metabolized
-
-
?
additional information
?
-
CYP79A1 has a very high substrate specificity, tyrosine being the only substrate found. Analogs 1-nitro-2-p-(hydroxyphenyl)ethane, N-hydroxytyrosine and phenylalanine are able to bind to the enzyme, without being metabolized
-
-
?
additional information
?
-
product of the second N-hydroxylation reaction is N,N-dihydroxytyrosine. N,N-dihydroxytyrosine is dehydrated to 2-nitroso-3-(4-hydroxyphenyl) propionic acid which decarboxylates to p-hydroxyphenylacetaldehyde oxime. The dehydration and decarboxylation reactions may proceed non-enzymatically. The E/Z ratio of the p-hydroxyphenylacetaldehyde oxime produced by reconstituted cytochrome P450Tyr is 69:31. Binding of L-tyrosine or N-hydroxytyrosine mutually excludes binding of the other substrate
-
-
?
additional information
?
-
-
product of the second N-hydroxylation reaction is N,N-dihydroxytyrosine. N,N-dihydroxytyrosine is dehydrated to 2-nitroso-3-(4-hydroxyphenyl) propionic acid which decarboxylates to p-hydroxyphenylacetaldehyde oxime. The dehydration and decarboxylation reactions may proceed non-enzymatically. The E/Z ratio of the p-hydroxyphenylacetaldehyde oxime produced by reconstituted cytochrome P450Tyr is 69:31. Binding of L-tyrosine or N-hydroxytyrosine mutually excludes binding of the other substrate
-
-
?
additional information
?
-
no substrate: L-3,4-Dihydroxyphenyl-alanine, i.e. DOPA
-
-
?
additional information
?
-
no substrate: L-3,4-Dihydroxyphenyl-alanine, i.e. DOPA
-
-
?
additional information
?
-
-
no substrate: L-3,4-Dihydroxyphenyl-alanine, i.e. DOPA
-
-
?
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NATURAL SUBSTRATE
NATURAL 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-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase]
(E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O
-
overall reaction
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
N,N-dihydroxy-L-tyrosine
(E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
-
-
-
?
N-hydroxy-L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N,N-dihydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
L-tyrosine + O2 + [reduced NADPH-hemoprotein reductase]
N-hydroxy-L-tyrosine + [oxidized NADPH-hemoprotein reductase] + H2O
-
enzyme in biosynthesis of cyanogenic glucosides
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
glutathione
-
3 mM glutathione stimulates activity of the reconstituted enzyme
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.
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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
0.82
L-tyrosine
-
purified recombinant enzyme, in 50 mM Tricine, pH 7.9, a 30°C
5.83
L-tyrosine
-
unpurified recombinant enzyme in Escherichia coli membranes, in 50 mM Tricine, pH 7.9, a 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
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
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
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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
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
multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima
physiological function
multifunctional N-hydroxylase catalyzing the conversion of tyrosine to 4-hydroxyphenylacetaldoxime in the biosynthesis of the two cyanogenic glucosides taxiphyllin and triglochinin in Triglochin maritima. When CYP79E1 is reconstituted with CYP71E1 and NADPH-cytochrome P450 oxidoreductase from Sorghum bicolor, efficient conversion of tyrosine to p-hydroxymandelonitrile is observed
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
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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). C79A1_SORBI
558
1
61887
Swiss-Prot
Secretory Pathway (Reliability: 4)
B9T7E4_RICCO
338
1
38703
TrEMBL
Secretory Pathway (Reliability: 5)
B9SBS2_RICCO
329
1
37099
TrEMBL
Secretory Pathway (Reliability: 3)
A0A396GLQ7_MEDTR
144
0
16483
TrEMBL
other Location (Reliability: 3)
B9SBR9_RICCO
370
1
41404
TrEMBL
other Location (Reliability: 4)
B9SBR6_RICCO
390
1
43699
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
61700
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no modification
no posttranslational modifications at the N- and C-terminal ends except for the N-terminal methionine removal
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutant 1: first codons of Escherichia coli mRNA are enriched for A's and T's, second codon is changed into GCT, first 8 codons of P450 sequence are replaced with the N-terminal sequence of bovine P45017alpha, mutant 2: deletion of 14 amino acids, mutant 3: deletion of 25 amino acids, mutant 4: deletion of 75 amino acids
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
combined use of Renex 690, CHAPS and RTX-100 is optimal for maximal recovery and avoidance of conversion into cytochrome P-420
-
DEAE-Speharose column chromatography and Reactive Red-120 agarose column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
lipid micelles made from L-alpha-dilauroyl phosphatidylcholine are more than twice as effective in reconstituting cytochrome P-450Tyr activity as compared to other lipids
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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 (Nicotiana tabacum) 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. Transgenic tobacco and Arabidopsis plants expressing only CYP79A1 accumulate the same 4-hydroxyphenylacetaldoxime-derived products as transgenic plants expressing both sorghum cytochrome P450 enzymes. The transgenic CYP79A1 Arabidopsis plants accumulate large amounts of 4-hydroxybenzyl glucosinolate
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 0.10.2% 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
Halkier, B.A.; Moller, B.L.
The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate
J. Biol. Chem.
265
21114-21121
1990
Sorghum bicolor, Sorghum bicolor (Q43135)
brenda
Libbesen, O.; Koch, B.; Halkier, B.A.; Moller, B.L.
Isolation of the heme-thiolate enzyme chytochrome P-450tyr, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
Proc. Natl. Acad. Sci. USA
91
9740-9744
1994
Sorghum bicolor
brenda
Koch, B.M.; Sibbesen, O.; Halkier B.A.; Svendsen, I.; Mller B.L.
The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
Arch. Biochem. Biophys.
323
177-186
1995
Sorghum bicolor (Q43135), Sorghum bicolor
brenda
Halkier, B.A.; Nielsen, H.L.; Koch, B.; Moller B.L.
Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli
Arch. Biochem. Biophys.
322
369-377
1995
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, Sorghum bicolor (Q43135)
brenda
Bak, S.; Nielsen, H.L.; Halkier, B.A.
The presence of CYP79 homologues in glucosinolate-producing plants shows evolutionary conservation of the enzymes in the conversion of amino acid to aldoxime in the biosynthesis of cyanogenic clucosides and glucosinolates
Plant Mol. Biol.
38
725-734
1998
Sinapis alba
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 (Q43135)
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 (Q43135), 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 (Q43135)
brenda
Sibbesen, O.; Koch, B.; Halkier, B.; Moller, B.
Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench
J. Biol. Chem.
270
3506-3511
1995
Sorghum bicolor (Q43135), Sorghum bicolor
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 (Q43135)
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 (Q43135)
brenda
Nielsen, J.; Moller, B.
Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima
Plant Physiol.
122
1311-1321
2000
Triglochin maritima (Q9M7B9), Triglochin maritima (Q9M7C0), Triglochin maritima
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 (Q43135)
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 (Q43135), Sorghum bicolor
brenda
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