| EC |
2.1.3.3 |
| Accepted name: |
ornithine carbamoyltransferase |
| Reaction: |
carbamoyl phosphate + L-ornithine = phosphate + L-citrulline |
|
For diagram of the urea cycle and arginine biosynthesis, click here |
| Other name(s): |
citrulline phosphorylase; ornithine transcarbamylase; OTC; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase |
| Systematic name: |
carbamoyl-phosphate:L-ornithine carbamoyltransferase |
| Comments: |
The plant enzyme also catalyses the reactions of EC 2.1.3.6 putrescine carbamoyltransferase, EC 2.7.2.2 carbamate kinase and EC 3.5.3.12 agmatine deiminase, thus acting as putrescine synthase, converting agmatine [(4-aminobutyl)guanidine] and ornithine into putrescine and citrulline, respectively. |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-69-8 |
| References: |
| 1. |
Bishop, S.H. and Grisolia, S. Crystalline ornithine transcarbamylase. Biochim. Biophys. Acta 139 (1967) 344–348. [DOI] [PMID: 6034676] |
| 2. |
Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure. J. Biol. Chem. 247 (1972) 1641–1653. [PMID: 4622303] |
| 3. |
Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. II. Multiple binding sites for carbamyl-P and L-norvaline, correlation with steady state kinetics. J. Biol. Chem. 247 (1972) 1654–1668. [PMID: 4622304] |
| 4. |
Marshall, M. and Cohen, P.P. Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. 3. Effects of chemical modifications of specific residues on ligand binding and enzymatic activity. J. Biol. Chem. 247 (1972) 1669–1682. [PMID: 4622305] |
|
| [EC 2.1.3.3 created 1961] |
| |
|
| |
|
Printable version