EC number:4.2.3.4
| ID: | 4.2.3.4 |
|---|---|
| Description: | 3-dehydroquinate synthase. |
| Alternative Name: |
Dehydroquinate synthase. 5-dehydroquinic acid synthetase. 5-dehydroquinate synthase. 3-dehydroquinate synthetase. |
| Cath: | 1.20.1090.10; 3.20.20.70; 3.40.50.1970; |
3D structure
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.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 4.2.3.4 |
| BRENDA Enzyme Link: | BRENDA 4.2.3.4 |
| KEGG Enzyme Link: | KEGG4.2.3.4 |
| BioCyc Enzyme Link: | BioCyc 4.2.3.4 |
| ExPASy Enzyme Link: | ExPASy4.2.3.4 |
| EC2PDB Enzyme Link: | EC2PDB 4.2.3.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.2.3.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.2.3.4 |
| IntEnz Enzyme Link: | IntEnz 4.2.3.4 |
| MEDLINE Enzyme Link: | MEDLINE 4.2.3.4 |
| RHEA:21968 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate |
| RULE(radius=1) | [*:1]-[O;H0;+0:2]-[CH2;+0:3]-[*:4]-[*:5]-[CH;+0:6](-[OH;+0:7])-[*:8]-[C;H0;+0:9](-[*:10])=[O;H0;+0:11]>>[*:10]-[C;H0;+0:9]1(-[OH;+0:11])-[*:8]-[C;H0;+0:6](=[O;H0;+0:7])-[*:5]-[*:4]-[CH2;+0:3]-1.[*:1]-[OH;+0:2] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. | Carpenter EP, Hawkins AR, Frost JW, Brown KA | 1998 Jul 16 | 9685163 |
| Mechanism and stereochemistry of 5-dehydroquinate synthetase. | Rotenberg SL, Sprinson DB | 1970 Dec | 5275368 |
| Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. | Bender SL, Mehdi S, Knowles JR | 1989 Sep 19 | 2514789 |
| Kinetic mechanism determination and analysis of metal requirement of dehydroquinate synthase from Mycobacterium tuberculosis H37Rv: an essential step in the function-based rational design of anti-TB drugs. | de Mendonça JD, Adachi O, Rosado LA, Ducati RG, Santos DS, Basso LA | 2011 Jan | 20978656 |