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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 1.3.98.3

Accepted Name
Coproporphyrinogen dehydrogenase.
Alternative Name(s)
Coproporphyrinogen III oxidase.
Oxygen-independent coproporphyrinogen-III oxidase.
Reaction catalysed
Coproporphyrinogen III + 2 S-adenosyl-L-methionine <=> protoporphyrinogen IX + 2 CO(2) + 2 L-methionine + 2 5'-deoxyadenosine
Cofactor(s)
Iron-sulfur.
Comment(s)
  • Differs from EC 1.3.3.3 by using S-adenosyl-L-methionine (AdoMet) instead of oxygen as oxidant.
  • 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-CH(2)-COO- -> -CH=CH(2) + CO(2) + e(-) replaces the electron initially used.
  • Formerly EC 1.3.99.22.
Cross-references
BRENDA1.3.98.3
EC2PDB1.3.98.3
ExplorEnz1.3.98.3
PRIAM enzyme-specific profiles1.3.98.3
KEGG Ligand Database for Enzyme Nomenclature1.3.98.3
IUBMB Enzyme Nomenclature1.3.98.3
IntEnz1.3.98.3
MEDLINEFind literature relating to 1.3.98.3
MetaCyc1.3.98.3
UniProtKB/Swiss-Prot
P33770, HEMF_RHOS4;  O67886, HEMN_AQUAE;  O31381, HEMN_BRADU;  
O34162, HEMN_CUPNH;  P32131, HEMN_ECOLI;  Q9ZLH0, HEMN_HELPJ;  
O25376, HEMN_HELPY;  P95506, HEMN_MANHA;  Q51676, HEMN_PARDP;  
P77915, HEMN_PSEAE;  P51008, HEMN_RHOS4;  P95651, HEMN_RHOS5;  
P0A1E2, HEMN_SALTI;  P0A1E1, HEMN_SALTY;  P74132, HEMN_SYNY3;  
O31067, HEMN_THEVL;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.3.98.-
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