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Information on EC 1.3.98.3 - coproporphyrinogen dehydrogenase

for references in articles please use BRENDA:EC1.3.98.3

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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.

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

Synonyms
viperin, radical sam enzyme, oxygen-independent coproporphyrinogen iii oxidase, anaerobic coproporphyrinogen iii oxidase, athemn1, sll1876, sll1917, at5g63290, oxygen-independent cpo, oxygen-independent coproporphyrinogen-iii oxidase, 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
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