1.3.98.3: coproporphyrinogen dehydrogenase

This is an abbreviated version!
For detailed information about coproporphyrinogen dehydrogenase, go to the full flat file.

Word Map on EC 1.3.98.3

Reaction

Coproporphyrinogen III
+ 2 S-adenosyl-L-methionine =
protoporphyrinogen IX
+ 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine

Synonyms

anaerobic coproporphyrinogen III oxidase, At5g63290, AtHEMN1, BtrN, Coprogen oxidase, coproporphyrinogen III oxidase, coproporphyrinogen oxidase, coproporphyrinogenase, CPO, HemN, HEMN1, HemW, More, oxidase, coproporphyrinogen, oxygen-independent coproporphyrinogen III oxidase, oxygen-independent coproporphyrinogen-III oxidase, oxygen-independent CPO, radical S-adenosyl-L-methionine dehydrogenase, radical SAM enzyme, Sll1876, Sll1917, viperin

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.98 With other, known, physiological acceptors
                1.3.98.3 coproporphyrinogen dehydrogenase

Systematic Name

Systematic Name on EC 1.3.98.3 - coproporphyrinogen dehydrogenase

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SYSTEMATIC NAME
IUBMB Comments
coproporphyrinogen-III:S-adenosyl-L-methionine oxidoreductase (decarboxylating)
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.