EC number:1.14.14.36
Enzyme
Download| 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 |
| ID: | 1.14.14.36 | ||
|---|---|---|---|
| Description: | Tyrosine N-monooxygenase. | ||
| Alternative Name: |
Tyrosine N-hydroxylase. CYP79A1. | ||
| Prosite: | PDOC00081; | ||
| PDB: |
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3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.36 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.36 |
| KEGG Enzyme Link: | KEGG1.14.14.36 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.36 |
| ExPASy Enzyme Link: | ExPASy1.14.14.36 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.36 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.36 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.36 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.36 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.36 |
EC number:1.14.14.36
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:32311 | L-tyrosine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] = (E)-4-hydroxyphenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2 oxidized [NADPH--hemoprotein reductase] |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[*:3]:[*:4]-[NH;+0:5]-[c;H0;+0:6](:[*:7]):[c;H0;+0:8]-1:[nH;+0:9]:[*:10].[*:11]:[nH;+0:12]:[c;H0;+0:13]1:[c;H0;+0:14](:[*:15])-[NH;+0:16]-[*:17]:[*:18]-[N;H0;+0:19]-1-[*:20].[*:21]=[C;H0;+0:22](-[OH;+0:23])-[CH;+0:24](-[*:25])-[NH2;+0:26].[O;H0;+0:27]=[O;H0;+0:28].[O;H0;+0:29]=[O;H0;+0:30]>>[*:25]-[CH;+0:24]=[N;H0;+0:26]-[OH;+0:27].[*:1]-[n;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[c;H0;+0:6](:[*:7])-[c;H0;+0:8]:1:[n;H0;+0:9]:[*:10].[*:11]:[n;H0;+0:12]:[c;H0;+0:13]1:[n;H0;+0:19](-[*:20]):[*:18]:[*:17]:[n;H0;+0:16]:[c;H0;+0:14]-1:[*:15].[*:21]=[C;H0;+0:22]=[O;H0;+0:23].[OH2;+0:28].[OH2;+0:29].[OH2;+0:30] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways. | Clausen M, Kannangara RM, Olsen CE, Blomstedt CK, Gleadow RM, Jørgensen K, Bak S, Motawie MS, Møller BL | 2015 Nov | 26361733 |
| Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. | Kristensen C, Morant M, Olsen CE, Ekstrøm CT, Galbraith DW, Møller BL, Bak S | 2005 Feb 1 | 15665094 |
| 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. | Sibbesen O, Koch B, Halkier BA, Møller BL | 1995 Feb 24 | 7876084 |
| 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. | Halkier BA, Møller BL | 1990 Dec 5 | 2250015 |