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Literature summary extracted from

  • Layer, G.; Verfurth, K.; Mahlitz, E.; Jahn, D.
    Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli (2002), J. Biol. Chem., 277, 34136-34142.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.98.3 hemeN gene, overexpression in Escherichia coli BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.3.98.3 C62S inactive mutant, no Fe-S cluster formation Escherichia coli
1.3.98.3 C66S inactive mutant, no Fe-S cluster formation Escherichia coli
1.3.98.3 C69S inactive mutant, no Fe-S cluster formation Escherichia coli
1.3.98.3 C71S inactive mutant, same Fe-S cluster formation as in wild-type HemN Escherichia coli
1.3.98.3 F68L mutant with 89% of wild-type activity Escherichia coli
1.3.98.3 G111V/G113V double mutation of Gly-111 and Gly-113, which are part of the potential GGGTP S-adenosyl-L-methionine binding motif, completely abolishes enzyme activity, reduced Fe-S cluster formation Escherichia coli
1.3.98.3 H58L inactive mutant, no Fe-S cluster formation Escherichia coli
1.3.98.3 Y56F mutant with 45% of wild-type activity and reduced Fe-S cluster formation Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.98.3 EDTA strong inhibition Escherichia coli
1.3.98.3 o-phenanthroline strong inhibition Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.98.3 52000
-
 gel filtration in combination with glycerol gradient centrifugation Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.98.3 recombinant wild-type and mutant HemN 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 catalytic, radical mechanism Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.98.3 coproporphyrinogen-III + S-adenosyl-L-methionine HemN catalyzes the oxygen-independent conversion of coproporphyrinogen-III to protoporphyrinogen IX, requires S-adenosyl-L-methionine, NAD(P)H and additional cytoplasmatic components for catalysis. Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for iron-sulfur cluster formation and enzyme function. Gly-111 and Gly-113 are part of the potential GGGTP S-adenosyl-L-methionine binding motif and essential for enzymatic function, catalytic, radical mechanism Escherichia coli protoporphyrinogen IX + CO2 + L-methionine + 5'-deoxyadenosine
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.98.3 monomer 1* 52734, sequence calculation Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.3.98.3 More Radical SAM enzyme 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

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.98.3 4Fe-4S-center requirement, oxygen-sensitive Fe-S cluster, Cys-62, Cys-66 and Cys-69 are part of the conserved CXXXCXXC motif and essential for Fe-S cluster formation and enzyme function, Tyr-56 and His-58 are important for the Fe-S cluster integrity, His-58 may provide the fourth ligand besides the three cysteine residues Escherichia coli
1.3.98.3 NADH requires NAD(P)H, higher activity than with NADPH as cofactor Escherichia coli
1.3.98.3 NADPH requires NAD(P)H, lower activity than with NADH as cofactor Escherichia coli
1.3.98.3 S-adenosyl-L-methionine uses S-adenosyl-L-methionine as a cofactor Escherichia coli