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ENZYME

ENZYME entry: EC 1.3.98.3

PURL: https://purl.expasy.org/enzyme/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 5'-deoxyadenosine + 2 L-methionine + 2 CO2
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-CH2-COO- -> -CH=CH2 + CO2 + 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
KEGG Ligand Database for Enzyme Nomenclature1.3.98.3
IUBMB Enzyme Nomenclature1.3.98.3
MEDLINEFind literature relating to 1.3.98.3
MetaCyc1.3.98.3
Rhea expert-curated reactions1.3.98.3
UniProtKB/Swiss-Prot
P33770, HEMF_CERS4O67886, HEMN_AQUAEO31381, HEMN_BRADU
P51008, HEMN_CERS4P95651, HEMN_CERS5O34162, HEMN_CUPNH
P32131, HEMN_ECOLIQ9ZLH0, HEMN_HELPJO25376, HEMN_HELPY
P95506, HEMN_MANHAQ51676, HEMN_PARDPP77915, HEMN_PSEAE
P0A1E2, HEMN_SALTIP0A1E1, HEMN_SALTYP74132, HEMN_SYNY3
O31067, HEMN_THEVL

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