EC 2.1.3.3 - Ornithine carbamoyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.3.3

Names

Accepted name:
ornithine carbamoyltransferase
Other names:
L-ornithine carbamoyltransferase
L-ornithine carbamyltransferase
L-ornithine transcarbamylase
OTC
carbamylphosphate-ornithine transcarbamylase
citrulline phosphorylase
ornithine carbamyltransferase
ornithine transcarbamylase
Systematic name:
carbamoyl-phosphate:L-ornithine carbamoyltransferase

Reaction

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 and ornithine into putrescine and citrulline, respectively.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00091
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004585
CAS Registry Number: 9001-69-8
UniProtKB/Swiss-Prot: (406) [show] [UniProt]

References

  1. Bishop, S.H. and Grisolia, S.
    Crystalline ornithine transcarbamylase.
    Biochim. Biophys. Acta 139: 344-348 (1967).
  2. Marshall, M. and Cohen, P.P.
    Ornithine transcarbamylase from Streptococcus faecalis and bovine liver. I. Isolation and subunit structure.
    J. Biol. Chem. 247: 1641-1653 (1972). [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: 1654-1668 (1972). [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: 1669-1682 (1972). [PMID: 4622305]

[EC 2.1.3.3 created 1961]