EC number:2.1.3.9

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.3 Carboxy- and carbamoyltransferases
ID:2.1.3.9
Description:N-acetylornithine carbamoyltransferase.
Alternative Name: N-acetylornithine transcarbamylase.
AOTC.
Acetylornithine transcarbamylase.
Prosite: PDOC00091;
PDB:
PDBScop
Cath: 3.40.47.10; 3.40.50.1370;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.3.9
BRENDA Enzyme Link: BRENDA 2.1.3.9
KEGG Enzyme Link: KEGG2.1.3.9
BioCyc Enzyme Link: BioCyc 2.1.3.9
ExPASy Enzyme Link: ExPASy2.1.3.9
EC2PDB Enzyme Link: EC2PDB 2.1.3.9
ExplorEnz Enzyme Link: ExplorEnz 2.1.3.9
PRIAM enzyme-specific profiles Link: PRIAM 2.1.3.9
IntEnz Enzyme Link: IntEnz 2.1.3.9
MEDLINE Enzyme Link: MEDLINE 2.1.3.9

EC number:2.1.3.9

MSA:

2.1.3.9;
Phylogenetic Tree:

2.1.3.9;
Uniprot:
M-CSA:
RHEA:18609 carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)-acetyl-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
Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis.Morizono H, Cabrera-Luque J, Shi D, Gallegos R, Yamaguchi S, Yu X, Allewell NM, Malamy MH, Tuchman M2006 Apr16585758
Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several eubacteria.Shi D, Morizono H, Yu X, Roth L, Caldovic L, Allewell NM, Malamy MH, Tuchman M2005 Apr 1515731101