Cysteine dioxygenase

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. 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. CDO has been implicated in various neurodegenerative diseases and cancers, which is likely related to cysteine toxicity.

Cysteine dioxygenase
Human CDO (drawn from PDB 2IC1)
Identifiers
EC no.1.13.11.20
CAS no.37256-59-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
cysteine dioxygenase, type I
Cysteine dioxygenase 1, monomer, Human
Identifiers
SymbolCDO1
NCBI gene1036
HGNC1795
OMIM603943
RefSeqNM_001801
UniProtQ16878
Other data
EC number1.13.11.20
LocusChr. 5 q23.2
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StructuresSwiss-model
DomainsInterPro
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