| EC Tree |
| 2. Transferases |
| 2.3 Acyltransferases |
| 2.3.1 Transferring groups other than aminoacyl groups |
| ID: | 2.3.1.230 |
|---|---|
| Description: | 2-heptyl-4(1H)-quinolone synthase. |
| Cath: | 3.40.47.10; |
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 2.3.1.230 |
| BRENDA Enzyme Link: | BRENDA 2.3.1.230 |
| KEGG Enzyme Link: | KEGG2.3.1.230 |
| BioCyc Enzyme Link: | BioCyc 2.3.1.230 |
| ExPASy Enzyme Link: | ExPASy2.3.1.230 |
| EC2PDB Enzyme Link: | EC2PDB 2.3.1.230 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.3.1.230 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.3.1.230 |
| IntEnz Enzyme Link: | IntEnz 2.3.1.230 |
| MEDLINE Enzyme Link: | MEDLINE 2.3.1.230 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:50396 | (2-aminobenzoyl)acetate + H(+) + octanoyl-CoA = 2-heptyl-4-quinolone + CO2 + CoA + H2O |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[*:3]:[*:4]-[NH2;+0:5])-[CH2;+0:6]-[C;H0;+0:7](=[O;H0;+0:8])-[OH;+0:9].[*:10]=[C;H0;+0:11](-[CH2;+0:12]-[*:13])-[S;H0;+0:14]-[*:15].[H+;H0:16]>>[*:13]-[CH2;+0:12]-[c;H0;+0:7]1:[cH;+0:6]:[c;H0;+0:2](=[*:1]):[*:3]:[*:4]:[nH;+0:5]:1.[*:15]-[SH;+0:14].[*:10]=[C;H0;+0:11]=[O;H0;+0:8].[OH2;+0:9] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The end of an old hypothesis: the pseudomonas signaling molecules 4-hydroxy-2-alkylquinolines derive from fatty acids, not 3-ketofatty acids. | Dulcey CE, Dekimpe V, Fauvelle DA, Milot S, Groleau MC, Doucet N, Rahme LG, Lépine F, Déziel E | 2013 Dec 19 | 24239007 |
| PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM. | Drees SL, Li C, Prasetya F, Saleem M, Dreveny I, Williams P, Hennecke U, Emsley J, Fetzner S | 2016 Mar 25 | 26811339 |