Ornithine decarboxylase
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Ornithine decarboxylase
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| Identifiers | |
| Symbol | ODC1 |
| HUGO | 8109 |
| Entrez | 4953 |
| OMIM | 165640 |
| RefSeq | NM_002539 |
| UniProt | P11926 |
| PDB | 7odc |
| Other data | |
| EC number | 4.1.1.17 |
| Locus | Chr. 2 p25 |
The enzyme ornithine decarboxylase (ODC) is a homodimer of 461 amino acids (in humans, at least) that catalyzes the decarboxylation of ornithine producing, as a result, diamine putrescine. This is the first step and the rate limiting step in humans for the production of polyamines, compounds required for cell division. ODC gene expression is induced by a large number of biological stimuli including seizure activity in the brain.[citation needed]
ODC is the most well-characterized cellular protein subject to ubiquitin-independent proteasomal degradation. Although most proteins must first be tagged with multiple ubiquitin molecules before they are bound and degraded by the proteasome, ODC degradation is instead mediated by several recognition sites on the protein and its accessory factor antizyme 1. The ODC degradation process is regulated in a negative feedback loop by its reaction products. [1]
[edit] External link
[edit] References
- ^ Zhang M, Pickart CM, Coffino P. (2003). Determinants of proteasome recognition of ornithine decarboxylase, a ubiquitin-independent substrate. EMBO J 22(7):1488-96.
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Carboxy-lyases: Aromatic L-amino acid decarboxylase - Glutamate decarboxylase - Ornithine decarboxylase - Pyruvate decarboxylase - RuBisCO - Uridine monophosphate synthetase - Uroporphyrinogen III decarboxylase
