EC number:1.13.11.27
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases) |
| 1.13.11 With incorporation of two atoms of oxygen |
| ID: | 1.13.11.27 |
|---|---|
| Description: | 4-hydroxyphenylpyruvate dioxygenase. |
| Alternative Name: |
p-hydroxyphenylpyruvate oxidase. p-hydroxyphenylpyruvate dioxygenase. 4-hydroxyphenylpyruvate hydroxylase. |
| Cath: | 3.10.180.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.13.11.27 |
| BRENDA Enzyme Link: | BRENDA 1.13.11.27 |
| KEGG Enzyme Link: | KEGG1.13.11.27 |
| BioCyc Enzyme Link: | BioCyc 1.13.11.27 |
| ExPASy Enzyme Link: | ExPASy1.13.11.27 |
| EC2PDB Enzyme Link: | EC2PDB 1.13.11.27 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.13.11.27 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.13.11.27 |
| IntEnz Enzyme Link: | IntEnz 1.13.11.27 |
| MEDLINE Enzyme Link: | MEDLINE 1.13.11.27 |
EC number:1.13.11.27
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:16189 | 3-(4-hydroxyphenyl)pyruvate + O2 = CO2 + homogentisate |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4](=[*:5])-[*:6]-[*:7]1:[*:8]:[cH;+0:9]:[c;H0;+0:10](-[OH;+0:11]):[*:12]:[cH;+0:13]:1.[O;H0;+0:14]=[O;H0;+0:15]>>[*:5]=[C;H0;+0:4](-[OH;+0:11])-[*:6]-[*:7]1:[*:8]:[c;H0;+0:9](-[OH;+0:14]):[cH;+0:10]:[*:12]:[c;H0;+0:13]:1-[OH;+0:15].[*:1]=[C;H0;+0:2]=[O;H0;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity. | Lee MH, Zhang ZH, MacKinnon CH, Baldwin JE, Crouch NP | 1996 Sep 16 | 8814303 |
| Steady state kinetics of 4-hydroxyphenylpyruvate dioxygenase from human liver (III). | Rundgren M | 1977 Jul 25 | 873933 |
| Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874. | Lindstedt S, Rundgren M | 1982 Oct 25 | 7118918 |
| Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase. | Roche PA, Moorehead TJ, Hamilton GA | 1982 Jun | 7103516 |
| Intermediate partitioning kinetic isotope effects for the NIH shift of 4-hydroxyphenylpyruvate dioxygenase and the hydroxylation reaction of hydroxymandelate synthase reveal mechanistic complexity. | Shah DD, Conrad JA, Moran GR | 2013 Sep 3 | 23941465 |
| Evidence for the mechanism of hydroxylation by 4-hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase from intermediate partitioning in active site variants. | Shah DD, Conrad JA, Heinz B, Brownlee JM, Moran GR | 2011 Sep 6 | 21815644 |
| 4-hydroxyphenylpyruvate dioxygenase catalysis: identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme. | Raspail C, Graindorge M, Moreau Y, Crouzy S, Lefèbvre B, Robin AY, Dumas R, Matringe M | 2011 Jul 22 | 21613226 |
| Studies on a possible reaction intermediate of p-hydroxyphenylpyruvate dioxygenase. | Nakai C, Nozaki M, Hayaishi O | 1975 Nov 17 | 1239286 |