EC number:6.3.4.16
Enzyme
Download| EC Tree |
| 6. Ligases |
| 6.3 Forming carbon-nitrogen bonds |
| 6.3.4 Other carbon-nitrogen ligases |
| ID: | 6.3.4.16 | ||
|---|---|---|---|
| Description: | Carbamoyl-phosphate synthase (ammonia). | ||
| Alternative Name: |
CPS I. Carbon-dioxide--ammonia ligase. Carbamoylphosphate synthetase (ammonia). Carbamoylphosphate synthase (ammonia). Carbamoyl-phosphate synthetase I. Carbamoyl-phosphate synthetase (ammonia). | ||
| Prosite: | PDOC00676; | ||
| PDB: |
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| Cath: | 1.10.1030.10; 3.20.20.140; 3.30.1490.20; 3.30.470.20; 3.40.50.880; 3.50.30.20; 3.40.50.1370; 3.40.50.1380; 3.40.50.20; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 6.3.4.16 |
| BRENDA Enzyme Link: | BRENDA 6.3.4.16 |
| KEGG Enzyme Link: | KEGG6.3.4.16 |
| BioCyc Enzyme Link: | BioCyc 6.3.4.16 |
| ExPASy Enzyme Link: | ExPASy6.3.4.16 |
| EC2PDB Enzyme Link: | EC2PDB 6.3.4.16 |
| ExplorEnz Enzyme Link: | ExplorEnz 6.3.4.16 |
| PRIAM enzyme-specific profiles Link: | PRIAM 6.3.4.16 |
| IntEnz Enzyme Link: | IntEnz 6.3.4.16 |
| MEDLINE Enzyme Link: | MEDLINE 6.3.4.16 |
| RHEA:18029 | 2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate |
| RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[OH;+0:4].[*:5]=[P;H0;+0:6](-[*:7])(-[*:8])-[O;H0;+0:9]-[*:10].[*:11]=[P;H0;+0:12](-[*:13])(-[*:14])-[O;H0;+0:15]-[*:16].[NH3;+0:17]>>[*:10]-[OH;+0:9].[*:16]-[OH;+0:15].[*:11]=[P;H0;+0:12](-[*:13])(-[*:14])-[O;H0;+0:4]-[C;H0;+0:2](=[*:1])-[NH2;+0:17].[*:5]=[P;H0;+0:6](-[*:7])(-[*:8])-[OH;+0:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Human carbamylphosphate synthetase I. Stabilization, purification, and partial characterization of the enzyme from human liver. | Pierson DL, Brien JM | 1980 Aug 25 | 6249820 |
| Physical and Kinetic Properties of Carbamyl Phosphate Synthetase from Frog Liver. | Marshall M, Metzenberg RL, Cohen PP | 1961 Aug | 26151989 |
| Understanding carbamoyl phosphate synthetase (CPS1) deficiency by using the recombinantly purified human enzyme: effects of CPS1 mutations that concentrate in a central domain of unknown function. | Díez-Fernández C, Hu L, Cervera J, Häberle J, Rubio V | 2014 Jun | 24813853 |
| Molecular characterization of carbamoyl-phosphate synthetase (CPS1) deficiency using human recombinant CPS1 as a key tool. | Diez-Fernandez C, Martínez AI, Pekkala S, Barcelona B, Pérez-Arellano I, Guadalajara AM, Summar M, Cervera J, Rubio V | 2013 Aug | 23649895 |
| A KINETIC STUDY OF CARBAMYL PHOSPHATE SYNTHETASE. | FAHIEN LA, COHEN PP | 1964 Jun | 14213379 |
| The pathway of carbonate in the biosynthesis of carbamyl phosphate. | JONES ME, SPECTOR L | 1960 Oct | 13790558 |
| Purification of carbamyl phosphate synthetase from frog liver. | MARSHALL M, METZENBERG RL, COHEN PP | 1958 Jul | 13563449 |
| Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase. | Pekkala S, Martínez AI, Barcelona B, Gallego J, Bendala E, Yefimenko I, Rubio V, Cervera J | 2009 Nov 11 | 19754428 |