Oxidoreductases;
Acting on the CH-CH group of donors;
With other, known, physiological acceptors
BRITE hierarchy

coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)

coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine [RN:R06895]

R06895
Reaction

coproporphyrinogen III [CPD:C03263];
S-adenosyl-L-methionine [CPD:C00019]

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.

EC 1.3.98.3 created 2004 as EC 1.3.99.22, transferred 2016 to EC 1.3.98.3