EC number:3.5.1.6
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.6 | ||
|---|---|---|---|
| Description: | Beta-ureidopropionase. | ||
| Prosite: | PDOC50263; | ||
| PDB: |
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| Cath: | 3.30.70.360; 3.40.630.10; 3.60.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.6 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.6 |
| KEGG Enzyme Link: | KEGG3.5.1.6 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.6 |
| ExPASy Enzyme Link: | ExPASy3.5.1.6 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.6 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.6 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.6 |
| RHEA:37339 | 3-ureidoisobutyrate + 2 H(+) + H2O = (2R)-3-amino-2-methylpropanoate + CO2 + NH4(+) |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[NH2;+0:3])-[NH;+0:4]-[*:5].[H+;H0:6].[H+;H0:7].[OH2;+0:8]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2]=[O;H0;+0:8].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Clinical, biochemical and molecular analysis of 13 Japanese patients with β-ureidopropionase deficiency demonstrates high prevalence of the c.977G > A (p.R326Q) mutation [corrected]. | Nakajima Y, Meijer J, Dobritzsch D, Ito T, Meinsma R, Abeling NG, Roelofsen J, Zoetekouw L, Watanabe Y, Tashiro K, Lee T, Takeshima Y, Mitsubuchi H, Yoneyama A, Ohta K, Eto K, Saito K, Kuhara T, van Kuilenburg AB | 2014 Sep | 24526388 |
| RHEA:11184 | 3-ureidopropanoate + 2 H(+) + H2O = beta-alanine + CO2 + NH4(+) |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[NH2;+0:3])-[NH;+0:4]-[*:5].[H+;H0:6].[H+;H0:7].[OH2;+0:8]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2]=[O;H0;+0:8].[NH3;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Cloning, sequencing, and expression of a cDNA encoding beta-alanine synthase from rat liver. | Kvalnes-Krick KL, Traut TW | 1993 Mar 15 | 8449931 |
| Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay. | Traut TW, Loechel S | 1984 May 22 | 6433973 |
| 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 |
| beta-Ureidopropionase deficiency: an inborn error of pyrimidine degradation associated with neurological abnormalities. | van Kuilenburg AB, Meinsma R, Beke E, Assmann B, Ribes A, Lorente I, Busch R, Mayatepek E, Abeling NG, van Cruchten A, Stroomer AE, van Lenthe H, Zoetekouw L, Kulik W, Hoffmann GF, Voit T, Wevers RA, Rutsch F, van Gennip AH | 2004 Nov 15 | 15385443 |
| Yeast beta-alanine synthase shares a structural scaffold and origin with dizinc-dependent exopeptidases. | Lundgren S, Gojković Z, Piskur J, Dobritzsch D | 2003 Dec 19 | 14534321 |
| Eukaryotic beta-alanine synthases are functionally related but have a high degree of structural diversity. | Gojković Z, Sandrini MP, Piskur J | 2001 Jul | 11454750 |
| Characterization of plant beta-ureidopropionase and functional overexpression in Escherichia coli. | Walsh TA, Green SB, Larrinua IM, Schmitzer PR | 2001 Feb | 11161056 |