show all | hide all No of entries

Information on EC 1.3.98.3 - coproporphyrinogen dehydrogenase

for references in articles please use BRENDA:EC1.3.98.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This enzyme differs from EC 1.3.3.3, coproporphyrinogen oxidase, by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant. It occurs mainly in bacteria, whereas eukaryotes use the oxygen-dependent oxidase. The reaction starts by using an electron from the reduced form of the enzyme's [4Fe-4S] cluster to split AdoMet into methionine and the radical 5'-deoxyadenosin-5'-yl. This radical initiates attack on the 2-carboxyethyl groups, leading to their conversion into vinyl groups. This conversion, ---(.)CH-CH2-COO- -> ---CH=CH2 + CO2 + e- replaces the electron initially used.
Specify your search results
Select one or more organisms in this record:
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
viperin, radical sam enzyme, oxygen-independent coproporphyrinogen iii oxidase, athemn1, anaerobic coproporphyrinogen iii oxidase, sll1876, hemn1, sll1917, at5g63290, oxygen-independent cpo, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
show the reaction diagram
Select items on the left to see more content.