| Entry |
|
|---|
| Name |
tyrosine N-monooxygenase;
tyrosine N-hydroxylase;
CYP79A1 |
|---|
| Class |
Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or
reduction of oxygen. The oxygen incorporated need not be derived
from O2;
With NADH or NADPH as one donor, and incorporation of one atom of
oxygen into the other donor
 |
|---|
| Sysname |
L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating) |
|---|
| Reaction(IUBMB) |
(1) (1a) L-tyrosine + O2 + NADPH + H+ = N-hydroxy-L-tyrosine + NADP+
+ H2O [RN:R00730];
(2) (1b) N-hydroxy-L-tyrosine + O2 + NADPH + H+ =
N,N-dihydroxy-L-tyrosine + NADP+ + H2O [RN:R04460];
(3) (1c) N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde
oxime] + CO2 + H2O [RN:R07190] |
|---|
| Reaction(KEGG) |
R00730 R04460 R07190;
(other) R01260 R06585 R08656
 |
|---|
| Substrate |
L-tyrosine [CPD:C00082];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080];
N-hydroxy-L-tyrosine [CPD:C03004];
N,N-dihydroxy-L-tyrosine [CPD:C15503] |
|---|
| Product |
N-hydroxy-L-tyrosine [CPD:C03004];
NADP+ [CPD:C00006];
H2O [CPD:C00001];
N,N-dihydroxy-L-tyrosine [CPD:C15503];
(Z)-[4-hydroxyphenylacetaldehyde oxime];
CO2 [CPD:C00011] |
|---|
| Cofactor |
Heme [CPD:C00032] |
|---|
| Comment |
A heme-thiolate protein (P-450). This enzyme is involved in the
biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along
with EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase
and EC 2.4.1.85, cyanohydrin beta-glucosyltransferase. Some
2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product. |
|---|
| Pathway |
PATH: ec00460 Cyanoamino acid metabolism
PATH: ec00966 Glucosinolate biosynthesis
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K13027 tyrosine N-monooxygenase |
|---|
| Genes |
SBI: SORBI_01g001200(SORBIDRAFT_01g001200)
 |
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Reference
Authors
Title
Journal
Organism
|
1 [PMID:2250015]
Halkier BA, Moller BL.
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 (1990) 21114-21.
Sorghum bicolor [GN:sbi] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:7876084]
Sibbesen O, Koch B, Halkier BA, Moller BL.
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 (1995) 3506-11.
Sorghum bicolor [GN:sbi] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:10938360]
Bak S, Olsen CE, Halkier BA, Moller BL.
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 (2000) 1437-48.
Sorghum bicolor [GN:sbi] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:10759528]
Nielsen JS, Moller BL.
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 (2000) 1311-21.
Sorghum bicolor [GN:sbi] |
|---|
Reference
Authors
Title
Journal
Organism
|
5 [PMID:12114576]
Busk PK, Moller BL.
Dhurrin synthesis in sorghum is regulated at the transcriptional
level and induced by nitrogen fertilization in older plants.
Plant. Physiol. 129 (2002) 1222-31.
Sorghum bicolor [GN:sbi] |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:15665094]
Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller
BL, Bak S.
Metabolic engineering of dhurrin in transgenic Arabidopsis plants
with marginal inadvertent effects on the metabolome and
transcriptome.
Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 1779-84.
Sorghum bicolor [GN:sbi] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.14.13.41
IUBMB Enzyme Nomenclature: 1.14.13.41
ExPASy - ENZYME nomenclature database: 1.14.13.41
BRENDA, the Enzyme Database: 1.14.13.41
CAS: 159447-19-5 |
|---|
