EC number:2.1.3.3
Enzyme
Download| EC Tree |
| 2. Transferases |
| 2.1 Transferring one-carbon groups |
| 2.1.3 Carboxy- and carbamoyltransferases |
| ID: | 2.1.3.3 | ||
|---|---|---|---|
| Description: | Ornithine carbamoyltransferase. | ||
| Alternative Name: |
OTCase. OTC. Ornithine transcarbamylase. Citrulline phosphorylase. | ||
| Prosite: | PDOC00091; | ||
| PDB: |
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| Cath: | 3.75.10.10; 3.40.47.10; 3.40.50.1370; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.3.3 |
| BRENDA Enzyme Link: | BRENDA 2.1.3.3 |
| KEGG Enzyme Link: | KEGG2.1.3.3 |
| BioCyc Enzyme Link: | BioCyc 2.1.3.3 |
| ExPASy Enzyme Link: | ExPASy2.1.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.3.3 |
| IntEnz Enzyme Link: | IntEnz 2.1.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.3.3 |
| RHEA:19513 | carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate |
| RULE(radius=1) | [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[O;H0;+0:6]-[*:7]>>[*:1]-[NH;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[*:7]-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| 1.85-A resolution crystal structure of human ornithine transcarbamoylase complexed with N-phosphonacetyl-L-ornithine. Catalytic mechanism and correlation with inherited deficiency. | Shi D, Morizono H, Ha Y, Aoyagi M, Tuchman M, Allewell NM | 1998 Dec 18 | 9852088 |
| Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity. | Marshall M, Cohen PP | 1972 Mar 25 | 4622305 |
| Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics. | Marshall M, Cohen PP | 1972 Mar 25 | 4622304 |
| Site-directed mutagenesis of Escherichia coli ornithine transcarbamoylase: role of arginine-57 in substrate binding and catalysis. | Kuo LC, Miller AW, Lee S, Kozuma C | 1988 Nov 29 | 3072022 |