| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.2 In cyclic amides |
| ID: | 3.5.2.2 |
|---|---|
| Description: | Dihydropyrimidinase. |
| Alternative Name: |
Hydantoinase. |
| Cath: | 3.20.20.140; 3.30.70.360; 3.40.630.10; 3.60.110.10; 2.30.40.10; |
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 3.5.2.2 |
| BRENDA Enzyme Link: | BRENDA 3.5.2.2 |
| KEGG Enzyme Link: | KEGG3.5.2.2 |
| BioCyc Enzyme Link: | BioCyc 3.5.2.2 |
| ExPASy Enzyme Link: | ExPASy3.5.2.2 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.2.2 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.2.2 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.2.2 |
| IntEnz Enzyme Link: | IntEnz 3.5.2.2 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.2.2 |
| RHEA:37335 | 5,6-dihydrothymine + H2O = 3-ureidoisobutyrate + H(+) |
| RULE(radius=1) | [*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1].[OH2;+0:6]>>([*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6]).[H+;H0:7] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| RHEA:16121 | 5,6-dihydrouracil + H2O = 3-ureidopropanoate + H(+) |
| RULE(radius=1) | ([*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:4].[*:5]-[NH2;+0:6]).[H+;H0:7]>>[*:5]-[NH;+0:6]-[C;H0;+0:2](-[*:1])=[*:3].[OH2;+0:4] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme. | Brooks KP, Jones EA, Kim BD, Sander EG | 1983 Oct 15 | 6639068 |
| Dihydropyrimidine amidohydrolases and dihydroorotases share the same origin and several enzymatic properties. | Gojkovic Z, Rislund L, Andersen B, Sandrini MP, Cook PF, Schnackerz KD, Piskur J | 2003 Mar 15 | 12626710 |
| PYD2 encodes 5,6-dihydropyrimidine amidohydrolase, which participates in a novel fungal catabolic pathway. | Gojkovic Z, Jahnke K, Schnackerz KD, Piskur J | 2000 Jan 28 | 10656811 |
| A functional analysis of the pyrimidine catabolic pathway in Arabidopsis. | Zrenner R, Riegler H, Marquard CR, Lange PR, Geserick C, Bartosz CE, Chen CT, Slocum RD | 2009 | 19413687 |