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Literature summary extracted from

  • Breckau, D.; Mahlitz, E.; Sauerwald, A.; Layer, G.; Jahn, D.
    Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese (2003), J. Biol. Chem., 278, 46625-46631.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.3 overexpression of hemF oxygen-dependent enzyme form as N-terminally fusion protein with calmodulin-binding-peptide, overexpression of wild-type and mutant enzymes in strain BL21(DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
1.3.3.3 C167S site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 G127V site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 H106L site-directed mutagenesis, inactive mutant Escherichia coli
1.3.3.3 H145L site-directed mutagenesis, inactive mutant Escherichia coli
1.3.3.3 H175L site-directed mutagenesis, inactive mutant Escherichia coli
1.3.3.3 H96L site-directed mutagenesis, inactive mutant Escherichia coli
1.3.3.3 additional information mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity Escherichia coli
1.3.3.3 P133A site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 T132A site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 W123L site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 W124R site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 W166L site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 W274L site-directed mutagenesis, inactive mutant Escherichia coli
1.3.3.3 W298L site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 W36L site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 Y135F site-directed mutagenesis, activity similar to the wild-type Escherichia coli
1.3.3.3 Y160F site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 Y170F site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 Y213F site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 Y240F site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli
1.3.3.3 Y276F site-directed mutagenesis, activity and kinetics similar to the wild-type Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.3 EDTA
-
 Escherichia coli
1.3.3.3 EGTA
-
 Escherichia coli
1.3.3.3 additional information mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity Escherichia coli
1.3.3.3 protoporphyrin-IX inhibition of HemF Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.3 0.0016
-
 Coproporphyrinogen-III HemF mutant C167S Escherichia coli
1.3.3.3 0.002
-
 Coproporphyrinogen-III HemF mutant Y240F Escherichia coli
1.3.3.3 0.0021
-
 Coproporphyrinogen-III HemF mutant G127V Escherichia coli
1.3.3.3 0.0026
-
 Coproporphyrinogen-III recombinant O2-dependent enzyme form HemF Escherichia coli
1.3.3.3 0.003
-
 Coproporphyrinogen-III HemF mutants Y213F, T132A, and W166L Escherichia coli
1.3.3.3 0.0032
-
 Coproporphyrinogen-III HemF mutant W298L Escherichia coli
1.3.3.3 0.0033
-
 Coproporphyrinogen-III HemF mutant W123L Escherichia coli
1.3.3.3 0.0035
-
 Coproporphyrinogen-III HemF mutants Y160F, W123L, and P133A Escherichia coli
1.3.3.3 0.0036
-
 Coproporphyrinogen-III HemF mutant W124R Escherichia coli
1.3.3.3 0.0038
-
 Coproporphyrinogen-III HemF mutant Y135F Escherichia coli
1.3.3.3 0.0041
-
 Coproporphyrinogen-III HemF mutant Y170F Escherichia coli
1.3.3.3 0.0043
-
 Coproporphyrinogen-III HemF mutants Y276F and W36L Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.3.3 Mn2+ required, bound to the enzyme, stimulates, restores the enzyme inactivated by metal chelators, coordinated by residues His96, His106, His145, and His175 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.3 coproporphyrinogen-III + O2 Escherichia coli step in heme biosynthesis protoporphyrinogen-IX + CO2 + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.3 Escherichia coli
-
 oxygen-dependent and oxygen-independent enzymes, HemF and HemN
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.3 recombinant hemF oxygen-dependent enzyme form to homogeneity by affinity chromatography, the tag protein is cleaved off by thrombin, recombinant wild-type and mutant enzymes Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.3.3 coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O 2 possible catalytic pathways of the reaction, overview, Tyrp274 is catalytically important, the following residues are not important for enzyme activity: Cys167, Tyr135, Tyr160, Tyr170, Tyr213, Tyr240, Tyr276, Trp36, Trp123, Trp166, and Trp198 Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.3 coproporphyrinogen-III + O2 step in heme biosynthesis Escherichia coli protoporphyrinogen-IX + CO2 + H2O
-
 ?
1.3.3.3 coproporphyrinogen-III + O2 HemF is absolutely dependent on oxygen Escherichia coli protoporphyrinogen-IX + CO2 + H2O
-
 ?
1.3.3.3 additional information no activity of HemF with protoporphyrinogen-IX and coporphyrinogen-III Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.3.3 coproporphyrinogen III oxidase
-
 Escherichia coli
1.3.3.3 CPO
-
 Escherichia coli
1.3.3.3 HemF
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.3.3.3 37
-
 assay at Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.3 0.003
-
 Coproporphyrinogen-III recombinant O2-dependent enzyme form Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.3 6
-
 recombinant O2-dependent enzyme form Escherichia coli