EC 2.1.3.11 - N-succinylornithine carbamoyltransferase

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IntEnz Enzyme Nomenclature
EC 2.1.3.11

Names

Accepted name:
N-succinylornithine carbamoyltransferase
Other names:
succinylornithine transcarbamylase
N-succinyl-L-ornithine transcarbamylase
SOTCase
Systematic name:
carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase

Reaction

Comments:

This enzyme is specific for N-succinyl-L-ornithine and cannot use either L-ornithine (see EC 2.1.3.3, ornithine carbamoyltransferase) or N-acetyl-L-ornithine (see EC 2.1.3.9, N-acetylornithine carbamoyltransferase) as substrate. However, a single amino-acid substitution (Pro90 → Glu90) is sufficient to switch the enzyme to one that uses N-acetyl-L-ornithine as substrate. It is essential for de novo arginine biosynthesis in the obligate anaerobe Bacteroides fragilis, suggesting that this organism uses an alternative pathway for synthesizing arginine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00091
Structural data: CSA , EC2PDB

References

  1. Shi, D., Morizono, H., Cabrera-Luque, J., Yu, X., Roth, L., Malamy, M. H., Allewell, N.M. and Tuchman, M.
    Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.
    J. Biol. Chem. 281: 20623-20631 (2006). [PMID: 16704984]
  2. Shi, D., Yu, X., Cabrera-Luque, J., Chen, T.Y., Roth, L., Morizono, H., Allewell, N.M. and Tuchman, M.
    A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.
    Protein Sci. 16: 1689-1699 (2007). [PMID: 17600144]

[EC 2.1.3.11 created 2008]