| 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: | 1.13.11.3 | ||
|---|---|---|---|
| Description: | Protocatechuate 3,4-dioxygenase. | ||
| Alternative Name: |
Protocatechuate oxygenase. | ||
| Prosite: | PDOC00079; | ||
| PDB: |
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| Cath: | 2.60.130.10; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.13.11.3 |
| BRENDA Enzyme Link: | BRENDA 1.13.11.3 |
| KEGG Enzyme Link: | KEGG1.13.11.3 |
| BioCyc Enzyme Link: | BioCyc 1.13.11.3 |
| ExPASy Enzyme Link: | ExPASy1.13.11.3 |
| EC2PDB Enzyme Link: | EC2PDB 1.13.11.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.13.11.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.13.11.3 |
| IntEnz Enzyme Link: | IntEnz 1.13.11.3 |
| MEDLINE Enzyme Link: | MEDLINE 1.13.11.3 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:10084 | 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 H(+) |
| RULE(radius=1) | [*:1]-[c;H0;+0:2]1:[cH;+0:3]:[c;H0;+0:4](-[OH;+0:5]):[c;H0;+0:6](-[OH;+0:7]):[cH;+0:8]:[cH;+0:9]:1.[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[C;H0;+0:2](=[CH;+0:3]-[C;H0;+0:4](=[O;H0;+0:5])-[OH;+0:11])-[CH;+0:9]=[CH;+0:8]-[C;H0;+0:6](=[O;H0;+0:7])-[OH;+0:10] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding. | Orville AM, Lipscomb JD, Ohlendorf DH | 1997 Aug 19 | 9254600 |
| Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications. | Que L Jr, Lipscomb JD, Münck E, Wood JM | 1977 Nov 23 | 199266 |
| Mechanism for catechol ring cleavage by non-heme iron intradiol dioxygenases: a hybrid DFT study. | Borowski T, Siegbahn PE | 2006 Oct 4 | 17002391 |