Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.12
Description:Ornithine cyclodeaminase.
Alternative Name: Ornithine cyclase (deaminating).
Ornithine cyclase.
OCD.
Cath: 3.30.1780.10; 3.40.50.720;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.12
BRENDA Enzyme Link: BRENDA 4.3.1.12
KEGG Enzyme Link: KEGG4.3.1.12
BioCyc Enzyme Link: BioCyc 4.3.1.12
ExPASy Enzyme Link: ExPASy4.3.1.12
EC2PDB Enzyme Link: EC2PDB 4.3.1.12
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.12
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.12
IntEnz Enzyme Link: IntEnz 4.3.1.12
MEDLINE Enzyme Link: MEDLINE 4.3.1.12
MSA:

4.3.1.12;

Phylogenetic Tree:

4.3.1.12;

Uniprot:
M-CSA:
RHEA:24368 L-ornithine = L-proline + NH4(+)
RULE(radius=1) ([*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[NH2;+0:6])>>[*:1]-[CH;+0:2](-[*:3])-[NH;+0:6]-[*:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Ornithine cyclase (deaminating). Purification of a protein that converts ornithine to proline and definition of the optimal assay conditions.Costilow RN, Laycock L1971 Nov4399881
Ornithine cyclase (deaminating). III. Mechanism of the conversion of ornithine to proline.Muth WL, Costilow RN1974 Dec 104154941
Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family.Goodman JL, Wang S, Alam S, Ruzicka FJ, Frey PA, Wedekind JE2004 Nov 915518536
Crystallization and X-ray diffraction analysis of ornithine cyclodeaminase from Pseudomonas putida.Alam S, Wang SC, Ruzicka FJ, Frey PA, Wedekind JE2004 May15103146