EC number:2.1.3.11

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.3 Carboxy- and carbamoyltransferases
ID:2.1.3.11
Description:N-succinylornithine carbamoyltransferase.
Alternative Name: Succinylornithine transcarbamylase.
SOTCase.
N-succinyl-L-ornithine transcarbamylase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.3.11
BRENDA Enzyme Link: BRENDA 2.1.3.11
KEGG Enzyme Link: KEGG2.1.3.11
BioCyc Enzyme Link: BioCyc 2.1.3.11
ExPASy Enzyme Link: ExPASy2.1.3.11
EC2PDB Enzyme Link: EC2PDB 2.1.3.11
ExplorEnz Enzyme Link: ExplorEnz 2.1.3.11
PRIAM enzyme-specific profiles Link: PRIAM 2.1.3.11
IntEnz Enzyme Link: IntEnz 2.1.3.11
MEDLINE Enzyme Link: MEDLINE 2.1.3.11

EC number:2.1.3.11

MSA:

2.1.3.11;
Phylogenetic Tree:

2.1.3.11;
Uniprot:
M-CSA:
RHEA:25884 carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-succinyl-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

TitleAuthorsDatePubMed ID
A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.Shi D, Yu X, Cabrera-Luque J, Chen TY, Roth L, Morizono H, Allewell NM, Tuchman M2007 Aug17600144
Structure and catalytic mechanism of a novel N-succinyl-L-ornithine transcarbamylase in arginine biosynthesis of Bacteroides fragilis.Shi D, Morizono H, Cabrera-Luque J, Yu X, Roth L, Malamy MH, Allewell NM, Tuchman M2006 Jul 2116704984