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Literature summary extracted from

  • Rand, K.; Noll, C.; Schiebel, H.M.; Kemken, D.; Duelcks, T.; Kalesse, M.; Heinz, D.W.; Layer, G.
    The oxygen-independent coproporphyrinogen III oxidase HemN utilizes harderoporphyrinogen as a reaction intermediate during conversion of coproporphyrinogen III to protoporphyrinogen IX (2010), Biol. Chem., 391, 55-63.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.98.3 gene hemN, expression in Escherichia coli strain BL21(DE3) Escherichia coli
1.3.98.3 recombinant expression as GST-fusion protein Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.98.3 H2O2 enzyme inactivation at 30% Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.98.3 Fe2+ HemN contains a catalytically essential [4Fe-4S] cluster that transfers an electron to bound S-adenosyl-L-methionine, thereby producing methionine and a 5'-deoxyadenosyl radical Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine Escherichia coli
-
 protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine Escherichia coli via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.98.3 Escherichia coli
-
-
-
1.3.98.3 Escherichia coli
-
 hemN
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.98.3 recombinant GST-tagged enzyme by glutathione affinity chromatography and ultrafiltration Escherichia coli
1.3.98.3 recombinant HemN from Escherichia coli strain BL21(DE3) Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine = protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen. HemN contains a catalytically essential [4Fe-4S] cluster that transfers an electron to bound S-adenosyl-L-methionine, thereby producing methionine and a 5'-deoxyadenosyl radical. This radical then abstracts a hydrogen atom from the beta-carbon of the substrate propionate side chain, resulting in the formation of a coproporphyrinogenyl radical, overview Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine
-
 Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine via reaction intermediate harderoporphyrinogen, not isoharderoporphyrinogen. During this reaction the propionate side chains on pyrrole rings A and B of coproporphyrinogen III are oxidatively decarboxylated to the corresponding vinyl groups of protoporphyrinogen IX. Two molecules of CO2 are released during the reaction and a final electron acceptor is required to take up two electrons from each side chain Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 coproporphyrinogen III + 2 S-adenosyl-L-methionine conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 harderoporphyrinogen + 2 S-adenosyl-L-methionine HemN can utilize chemically synthesized harderoporphyrinogen as a substrate and converts it to protoporphyrinogen IX Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
 ?
1.3.98.3 harderoporphyrinogen + S-adenosyl-L-methionine chemical substrate sythesis, overview Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.98.3 HemN
-
 Escherichia coli
1.3.98.3 oxygen-independent coproporphyrinogen III oxidase
-
 Escherichia coli
1.3.98.3 oxygen-independent CPO
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.98.3 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.98.3 7
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.98.3 S-adenosyl-L-methionine
-
 Escherichia coli
1.3.98.3 S-adenosyl-L-methionine HemN contains a catalytically essential [4Fe-4S] cluster that transfers an electron to bound S-adenosyl-L-methionine, thereby producing methionine and a 5'-deoxyadenosyl radical Escherichia coli

General Information

EC Number General Information Comment Organism
1.3.98.3 evolution in eukaryotes and some bacteria, oxidative decarboxylation of coproporphyrinogen III is performed by the oxygen-dependent CPO HemF, EC 1.3.3.3. In most bacteria, the reaction is catalyzed by the oxygen-independent enzyme HemN. HemN belongs to the family of radical S-adenosyl-L-methionine enzymes. HemF and HemN are structurally completely unrelated and show different catalytic mechanisms, overview Escherichia coli