ornithine cyclodeaminase
{{infobox enzyme
| Name = ornithine cyclodeaminase
| EC_number = 4.3.1.12
| CAS_number = 9054-76-6
| GO_code = 0008473
| image =
| width =
| caption =
}}
The enzyme ornithine cyclodeaminase (EC 4.3.1.12) catalyzes the chemical reaction
File:Ornithine cyclodeaminase.svg
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is Lornithine ammonia-lyase (cyclizing; L-proline-forming). Other names in common use include ornithine cyclase, ornithine cyclase (deaminating), and L-ornithine ammonia-lyase (cyclizing). This enzyme participates in arginine and proline biosynthesis. It employs one cofactor, NAD+.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1U7H}} and {{PDB link|1X7D}}.
References
{{reflist|1}}
- {{cite journal |vauthors=Costilow RN, Laycock L | year = 1971 | title = Ornithine cyclase (deaminating). Purification of a protein that converts ornithine to proline and definition of the optimal assay conditions | journal = Journal of Biological Chemistry | volume = 246 | pages = 6655–60 | pmid = 4399881 | issue = 21 | doi = 10.1016/S0021-9258(19)34165-1 | doi-access = free }}
- {{cite journal |vauthors=Muth WL, Costilow RN | year = 1974 | title = Ornithine cyclase (deaminating). II. Properties of the homogeneous enzyme | journal = Journal of Biological Chemistry | volume = 249 | pages = 7457–62 | pmid = 4373469 | issue = 23 | doi = 10.1016/S0021-9258(19)81260-7 | doi-access = free }}
- {{cite journal |vauthors=Espineda CE, Linford AS, Devine D, Brusslan JA | year = 1999 | title = The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyll b synthesis in Arabidopsis thaliana | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | pages = 10507–11 | pmid = 10468639 | doi = 10.1073/pnas.96.18.10507 | issue = 18 | pmc = 17919 | bibcode = 1999PNAS...9610507E | doi-access = free }}
- {{cite journal |vauthors=Goodman JL, Wang S, Alam S, Ruzicka FJ, Frey PA, Wedekind JE | year = 2004 | title = Ornithine cyclodeaminase: structure, mechanism of action, and implications for the mu-crystallin family | journal = Biochemistry | volume = 43 | pages = 13883–91 | pmid = 15518536 | doi = 10.1021/bi048207i | issue = 44 }}
- {{cite journal |vauthors=Alam S, Wang SC, Ruzicka FJ, Frey PA, Wedekind JE | year = 2004 | title = Crystallization and X-ray diffraction analysis of ornithine cyclodeaminase from Pseudomonas putida | journal = Acta Crystallographica Section D | volume = 60 | pages = 941–4 | pmid = 15103146 | doi = 10.1107/S0907444904005256 | issue = Pt 5 }}
{{Carbon-nitrogen lyases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
Category:NADH-dependent enzymes
Category:Enzymes of known structure
{{enzyme-stub}}