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Literature summary for 1.3.98.3 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)

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine Escherichia coli
-
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli
-
hemN
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
coproporphyrinogen III + 2 S-adenosyl-L-methionine
-
Escherichia coli protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
?
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
-
?
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
-
?
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
-
?
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
-
?
harderoporphyrinogen + S-adenosyl-L-methionine chemical substrate sythesis, overview Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Escherichia coli
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

General Information Comment Organism
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