| Cysteine dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Human CDO (drawn from PDB 2IC1) | |||||||||
| Identifiers | |||||||||
| EC no. | 1.13.11.20 | ||||||||
| CAS no. | 37256-59-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| cysteine dioxygenase, type I | |||||||
|---|---|---|---|---|---|---|---|
 Cysteine dioxygenase 1, monomer, Human | |||||||
| Identifiers | |||||||
| Symbol | CDO1 | ||||||
| NCBI gene | 1036 | ||||||
| HGNC | 1795 | ||||||
| OMIM | 603943 | ||||||
| RefSeq | NM_001801 | ||||||
| UniProt | Q16878 | ||||||
| Other data | |||||||
| EC number | 1.13.11.20 | ||||||
| Locus | Chr. 5 q23.2 | ||||||
| |||||||
Cysteine dioxygenase (CDO) is a non-heme iron enzyme that catalyzes the conversion of L-cysteine to cysteine sulfinic acid (cysteine sulfinate). CDO plays an important role in cysteine catabolism, regulating intracellular levels of cysteine and responding changes in cysteine availability.[1] As such, CDO is highly regulated and undergoes large changes in concentration and efficiency. It oxidizes cysteine to the corresponding sulfinic acid by activation of dioxygen, although the exact mechanism of the reaction is still unclear. In addition to being found in mammals, CDO also exists in some yeast and bacteria, although the exact function is still unknown.[2][3] CDO has been implicated in various neurodegenerative diseases and cancers, which is likely related to cysteine toxicity.[1][2]
- ^ a b Stipanuk MH, Ueki I, Dominy JE, Simmons CR, Hirschberger LL (May 2009). "Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels". Amino Acids. 37 (1): 55–63. doi:10.1007/s00726-008-0202-y. PMC 2736881. PMID 19011731.
- ^ a b Joseph CA, Maroney MJ (August 2007). "Cysteine dioxygenase: structure and mechanism". Chemical Communications (32): 3338–49. doi:10.1039/B702158E. PMID 18019494.
- ^ Stipanuk MH, Simmons CR, Karplus PA, Dominy JE (June 2011). "Thiol dioxygenases: unique families of cupin proteins". Amino Acids. 41 (1): 91–102. doi:10.1007/s00726-010-0518-2. PMC 3136866. PMID 20195658.