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Literature summary extracted from

  • Maneli, M.H.; Corrigall, A.V.; Klump, H.H.; Davids, L.M.; Kirsch, R.E.; Meissner, P.N.
    Kinetic and physical characterisation of recombinant wild-type and mutant human protoporphyrinogen oxidases (2003), Biochim. Biophys. Acta, 1650, 10-21.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.3.4 expression of wild-type and mutant enzymes in Escherichia coli strain JM109 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.3.3.4 G11A site-directed mutagenesis, 0.02% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 G14A site-directed mutagenesis, 42.6% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 G9A site-directed mutagenesis, 0.52% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 H20P site-directed mutagenesis, 0.16% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 additional information identification of several mutations of the enzyme encoding gene, responsible for variegate porphyria, overview Homo sapiens
1.3.3.4 R168C site-directed mutagenesis, 17.5% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 R59I site-directed mutagenesis, 1.5% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 R59K site-directed mutagenesis, 37.6% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 R59S site-directed mutagenesis, 2.6% activity compared to the wild-type enzyme Homo sapiens
1.3.3.4 R59W site-directed mutagenesis, 0.28% activity compared to the wild-type enzyme, highly reduced FAD binding Homo sapiens
1.3.3.4 Y348C site-directed mutagenesis, 8.6% activity compared to the wild-type enzyme Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.4 acifluorfen inhibition potency with recombinant wild-type and mutant enzymes, overview Homo sapiens
1.3.3.4 bilirubin inhibition potency with recombinant wild-type and mutant enzymes, overview Homo sapiens
1.3.3.4 biliverdin IX hydrochloride inhibition potency with recombinant wild-type and mutant enzymes, overview Homo sapiens
1.3.3.4 methyl acifluorfen inhibition potency with recombinant wild-type and mutant enzymes, overview Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.4 0.00083
-
 protoporphyrinogen-IX recombinant mutant R59K, pH 8.2 Homo sapiens
1.3.3.4 0.00085
-
 protoporphyrinogen-IX recombinant wild-type enzyme and mutant G14A, pH 8.2 Homo sapiens
1.3.3.4 0.001
-
 protoporphyrinogen-IX recombinant mutant R168C, pH 8.2 Homo sapiens
1.3.3.4 0.00107
-
 protoporphyrinogen-IX recombinant mutant Y348, pH 7.8 Homo sapiens
1.3.3.4 0.00126
-
 protoporphyrinogen-IX recombinant mutant R59W, pH 8.2 Homo sapiens
1.3.3.4 0.0017
-
 protoporphyrinogen-IX recombinant mutant R59S, pH 8.2 Homo sapiens
1.3.3.4 0.00209
-
 protoporphyrinogen-IX recombinant mutant R59I, pH 8.2 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.3.4 mitochondrial inner membrane
-
 Homo sapiens 5743
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.4 51000
-
 x * 51000, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.4 protoporphyrinogen-IX + 3 O2 Homo sapiens penultimate enzyme in the heme biosynthesis, several mutations of the enzyme encoding gene are responsible for variegate porphyria protoporphyrin-IX + 3 H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.3.4 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.4 recombinant wild-type and mutant enzymes from Escherichia coli strain JM109, to homogeneity Homo sapiens

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.3.3.4 renaturation and refolding after thermal denaturation and unfolding at 75°C by cooling to 15°C, pH 7.2 Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.3.4 additional information
-
-
 Homo sapiens
1.3.3.4 0.62
-
 recombinant mutant Y348C Homo sapiens
1.3.3.4 1.26
-
 recombinant mutant R168C Homo sapiens
1.3.3.4 2.69
-
 recombinant mutant R59K Homo sapiens
1.3.3.4 3.04
-
 recombinant mutant G14A Homo sapiens
1.3.3.4 7.15
-
 recombinant wild-type enzyme Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.3.4 protoporphyrinogen-IX + 3 O2 penultimate enzyme in the heme biosynthesis, several mutations of the enzyme encoding gene are responsible for variegate porphyria Homo sapiens protoporphyrin-IX + 3 H2O2
-
 ?
1.3.3.4 protoporphyrinogen-IX + 3 O2 roles of 59 arginine residues and glycine residues in the flavin binding site in catalysis and cofactor binding Homo sapiens protoporphyrin-IX + 3 H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.3.4 ? x * 51000, SDS-PAGE Homo sapiens
1.3.3.4 More secondary structure analysis, wild-type and mutant enzymes, structure/function relationship mutant R59W Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.3.3.4 PPOX
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.3.3.4 40
-
 recombinant wild-type and mutants, stable at Homo sapiens
1.3.3.4 47.6
-
 50% inactivation of mutant R168C Homo sapiens
1.3.3.4 50.2
-
 50% inactivation of mutant Y348C Homo sapiens
1.3.3.4 53
-
 50% inactivation of mutant R59W Homo sapiens
1.3.3.4 54.2
-
 50% inactivation of mutant R59I Homo sapiens
1.3.3.4 56.3
-
 50% inactivation of mutant R59K Homo sapiens
1.3.3.4 56.8
-
 50% inactivation of recombinant wild-type enzyme Homo sapiens
1.3.3.4 57
-
 50% inactivation of mutant G14A Homo sapiens
1.3.3.4 60.3
-
 50% inactivation of mutant R59S Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.3.4 0.04
-
 protoporphyrinogen-IX recombinant mutant R59W, pH 8.2 Homo sapiens
1.3.3.4 0.15
-
 protoporphyrinogen-IX recombinant mutant R59I, pH 8.2 Homo sapiens
1.3.3.4 0.17
-
 protoporphyrinogen-IX recombinant mutant R59S, pH 8.2 Homo sapiens
1.3.3.4 0.53
-
 protoporphyrinogen-IX recombinant mutant Y348, pH 7.8 Homo sapiens
1.3.3.4 1.02
-
 protoporphyrinogen-IX recombinant mutant R168C, pH 8.2 Homo sapiens
1.3.3.4 2.57
-
 protoporphyrinogen-IX recombinant mutant R59K, pH 8.2 Homo sapiens
1.3.3.4 3.9
-
 protoporphyrinogen-IX recombinant mutant G14A, pH 8.2 Homo sapiens
1.3.3.4 5.95
-
 protoporphyrinogen-IX recombinant wild-type enzyme, pH 8.2 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.4 7.8
-
 mutant Y348C Homo sapiens
1.3.3.4 8.2
-
 except for mutant Y348C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.3.4 FAD required, binding site, structure, and mechanism, roles of 59 arginine residues and glycine residues in the flavin binding site in catalysis and cofactor binding Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.3.4 0.00011
-
 acifluorfen recombinant mutant R59I, pH 8.2 Homo sapiens
1.3.3.4 0.00018
-
 acifluorfen recombinant mutant R59K, pH 8.2 Homo sapiens
1.3.3.4 0.00023
-
 acifluorfen recombinant wild-type, pH 8.2 Homo sapiens
1.3.3.4 0.00027
-
 acifluorfen recombinant mutant R59S, pH 8.2 Homo sapiens
1.3.3.4 0.00031
-
 acifluorfen recombinant mutant G14A, pH 8.2 Homo sapiens
1.3.3.4 0.00033
-
 acifluorfen recombinant mutant R59W, pH 8.2 Homo sapiens
1.3.3.4 0.003
-
 acifluorfen recombinant mutant R168C, pH 8.2 Homo sapiens
1.3.3.4 0.00472
-
 acifluorfen recombinant mutant Y348C, pH 7.8 Homo sapiens