EC number:2.5.1.61
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.5 Transferring alkyl or aryl groups, other than methyl groups |
| 2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date) |
| ID: | 2.5.1.61 | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Description: | Hydroxymethylbilane synthase. | ||||||||||||||||||||
| Alternative Name: |
Uroporphyrinogen synthetase. Uroporphyrinogen synthase. Uroporphyrinogen I synthetase. Uroporphyrinogen I synthase. Pre-uroporphyrinogen synthase. Porphobilinogen deaminase. HMB-synthase. (hydrolyzing). (4-(2-carboxyethyl)-3-(carboxymethyl)pyrrol-2-yl)methyltransferase | ||||||||||||||||||||
| Prosite: | PDOC00461; | ||||||||||||||||||||
| PDB: |
» hide |
||||||||||||||||||||
| Cath: | 3.30.160.40; 3.40.190.10; 3.40.50.10090; |
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 2.5.1.61 |
| BRENDA Enzyme Link: | BRENDA 2.5.1.61 |
| KEGG Enzyme Link: | KEGG2.5.1.61 |
| BioCyc Enzyme Link: | BioCyc 2.5.1.61 |
| ExPASy Enzyme Link: | ExPASy2.5.1.61 |
| EC2PDB Enzyme Link: | EC2PDB 2.5.1.61 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.5.1.61 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.5.1.61 |
| IntEnz Enzyme Link: | IntEnz 2.5.1.61 |
| MEDLINE Enzyme Link: | MEDLINE 2.5.1.61 |
| RHEA:13185 | H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+) |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[NH2;+0:3].[*:4]:[cH;+0:5]:[*:6]:[*:7]-[CH2;+0:8]-[NH2;+0:9].[*:10]:[cH;+0:11]:[*:12]:[*:13]-[CH2;+0:14]-[NH2;+0:15].[*:16]:[cH;+0:17]:[*:18]:[*:19]-[CH2;+0:20]-[NH2;+0:21].[OH2;+0:22]>>[*:4]:[c;H0;+0:5](:[*:6]:[*:7]-[CH2;+0:8]-[c;H0;+0:11](:[*:10]):[*:12]:[*:13]-[CH2;+0:14]-[c;H0;+0:17](:[*:16]):[*:18]:[*:19]-[CH2;+0:20]-[OH;+0:22])-[CH2;+0:2]-[*:1].[NH3;+0:3].[NH3;+0:9].[NH3;+0:15].[NH3;+0:21] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Discovery that the assembly of the dipyrromethane cofactor of porphobilinogen deaminase holoenzyme proceeds initially by the reaction of preuroporphyrinogen with the apoenzyme. | Shoolingin-Jordan PM, Warren MJ, Awan SJ | 1996 Jun 1 | 8687374 |
| Evidence for participation of aspartate-84 as a catalytic group at the active site of porphobilinogen deaminase obtained by site-directed mutagenesis of the hemC gene from Escherichia coli. | Woodcock SC, Jordan PM | 1994 Mar 8 | 8117733 |
| Biosynthesis of the pigments of life: formation of the macrocycle. | Battersby AR, Fookes CJ, Matcham GW, McDonald E | 1980 May 1 | 6769048 |
| Studies on porphobilinogen deaminase and uroporphyrinogen 3 cosynthase from human erythrocytes. | Frydman RB, Feinstein G | 1974 Jun 18 | 4847568 |
| Structure of porphobilinogen deaminase reveals a flexible multidomain polymerase with a single catalytic site. | Louie GV, Brownlie PD, Lambert R, Cooper JB, Blundell TL, Wood SP, Warren MJ, Woodcock SC, Jordan PM | 1992 Sep 3 | 1522882 |
| Tetrapyrroles: the pigments of life. | Battersby AR | 2000 Dec | 11152419 |