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Literature summary for 1.3.3.4 extracted from

  • Meissner, P.N.; Dailey, T.A.; Hift, R.J.; Ziman, M.; Corrigall, A.V.; Roberts, A.G.; Meissner, D.M.; Kirsch, R.E.; Dailey, H.A.
    A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria (1996), Nature Genet., 13, 95-97.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R59W significantly decreased activity, causes variagate porphyria Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0017
-
protoporphyrinogen-IX wild type and R59W mutant enzyme Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoporphyrinogen-IX + 3 O2 Homo sapiens penultimate step of heme and chlorophyll biosynthesis protoporphyrin-IX + 3 H2O2
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoporphyrinogen-IX + 3 O2
-
Homo sapiens protoporphyrin-IX + 3 H2O2
-
?
protoporphyrinogen-IX + 3 O2 penultimate step of heme and chlorophyll biosynthesis Homo sapiens protoporphyrin-IX + 3 H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.00333
-
protoporphyrinogen-IX below 0.2/min, R59W mutant enzyme Homo sapiens
0.175
-
protoporphyrinogen-IX wild type enzyme Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD essential cofactor Homo sapiens