KEGG   ENZYME: 1.14.14.36
Entry
EC 1.14.14.36               Enzyme                                 
Name
tyrosine N-monooxygenase;
tyrosine N-hydroxylase;
CYP79A1
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
Sysname
L-tyrosine,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating)
Reaction(IUBMB)
L-tyrosine + 2 O2 + 2 [reduced NADPH---hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH---hemoprotein reductase] + CO2 + 3 H2O (overall reaction) [RN:R10671];
(1a) L-tyrosine + O2 + [reduced NADPH---hemoprotein reductase] = N-hydroxy-L-tyrosine + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R00730];
(1b) N-hydroxy-L-tyrosine + O2 + [reduced NADPH---hemoprotein reductase] = N,N-dihydroxy-L-tyrosine + [oxidized NADPH---hemoprotein reductase] + H2O [RN:R04460];
(1c) N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O [RN:R07190]
Reaction(KEGG)
Substrate
L-tyrosine [CPD:C00082];
O2 [CPD:C00007];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
N-hydroxy-L-tyrosine [CPD:C03004];
N,N-dihydroxy-L-tyrosine [CPD:C15503]
Product
(E)-[4-hydroxyphenylacetaldehyde oxime] [CPD:C04350];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
CO2 [CPD:C00011];
H2O [CPD:C00001];
N-hydroxy-L-tyrosine [CPD:C03004];
N,N-dihydroxy-L-tyrosine [CPD:C15503]
Comment
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.
History
EC 1.14.14.36 created 1992 as EC 1.14.13.41, modified 2001, modified 2005, transferred 2016 to EC 1.14.14.36
Pathway
ec00460  Cyanoamino acid metabolism
ec00966  Glucosinolate biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K13027  tyrosine N-monooxygenase
K20785  tyrosine N-monooxygenase
Genes
CPAP110808696
MING122082619
BDI100844404 100844710
ATS109735617 109735773 109747263 109761069 109761668 109761669 109761674 109762566 109763923 109773788 109784188 109784348
TDC119283854 119310652 119310656 119315677 119315988 119322151 119322220 119322360 119322455 119322484 119323745 119323781 119325453 119325576 119326042 119326092 119328753 119333344 119334570 119339130 119346579 119346580 119346581 119346582 119346584 119347383 119349993 119359139 119367488
TAES123039366 123040956 123048979 123058645 123074835 123082655 123115314 123115317 123121204 123126171 123129465 123129689 123130256 123133566 123133567 123133663 123138575 123138576 123141446 123153217 123153556 123153558 123158178 123167847 123170371 123171291 123184966
TUA125516067 125516660 125518600 125524712 125525533 125525885 125548685 125554390
SBI8061413 8061994
ZMA103638611
SITA101771875 101781613
SVS117851946 117853679
PVIR120668766 120669225 120671567
PHAI112889966
 » show all
Reference
1  [PMID:2250015]
  Authors
Halkier BA, Moller BL.
  Title
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.
  Journal
J Biol Chem 265:21114-21 (1990)
Reference
2  [PMID:7876084]
  Authors
Sibbesen O, Koch B, Halkier BA, Moller BL.
  Title
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.
  Journal
J Biol Chem 270:3506-11 (1995)
DOI:10.1074/jbc.270.8.3506
Reference
3  [PMID:12223771]
  Authors
Bennett RN, Kiddle G, Wallsgrove RM.
  Title
Involvement of Cytochrome P450 in Glucosinolate Biosynthesis in White Mustard (A Biochemical Anomaly).
  Journal
Plant Physiol 114:1283-1291 (1997)
DOI:10.1104/pp.114.4.1283
Reference
4  [PMID:10049494]
  Authors
Kahn RA, Fahrendorf T, Halkier BA, Moller BL.
  Title
Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench.
  Journal
Arch Biochem Biophys 363:9-18 (1999)
DOI:10.1006/abbi.1998.1068
Reference
5  [PMID:10938360]
  Authors
Bak S, Olsen CE, Halkier BA, Moller BL.
  Title
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.
  Journal
Plant Physiol 123:1437-48 (2000)
DOI:10.1104/pp.123.4.1437
Reference
6  [PMID:10759528]
  Authors
Nielsen JS, Moller BL
  Title
Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima.
  Journal
Plant Physiol 122:1311-21 (2000)
DOI:10.1104/pp.122.4.1311
  Sequence
Reference
7  [PMID:12114576]
  Authors
Busk PK, Moller BL.
  Title
Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants.
  Journal
Plant Physiol 129:1222-31 (2002)
DOI:10.1104/pp.000687
Reference
8  [PMID:15665094]
  Authors
Kristensen C, Morant M, Olsen CE, Ekstrom CT, Galbraith DW, Moller BL, Bak S.
  Title
Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome.
  Journal
Proc Natl Acad Sci U S A 102:1779-84 (2005)
DOI:10.1073/pnas.0409233102
Reference
9  [PMID:26361733]
  Authors
Clausen M, Kannangara RM, Olsen CE, Blomstedt CK, Gleadow RM, Jorgensen K, Bak S, Motawie MS, Moller BL
  Title
The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways.
  Journal
Plant J 84:558-73 (2015)
DOI:10.1111/tpj.13023
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.36
IUBMB Enzyme Nomenclature: 1.14.14.36
ExPASy - ENZYME nomenclature database: 1.14.14.36
BRENDA, the Enzyme Database: 1.14.14.36
CAS: 159447-19-5

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