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Literature summary extracted from

  • Gabler, T.; Sebastiani, F.; Helm, J.; Dali, A.; Obinger, C.; Furtmueller, P.G.; Smulevich, G.; Hofbauer, S.
    Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups (2022), FEBS J., 289, 1680-1699.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
4.99.1.9 additional information all the non-wild-type LmCpfC variants prove to have a significantly higher koff and consequently a lower affinity. This weaker binding is also reflected in the kon-rate, which is the highest for both tested porphyrin ligands for the wild-type protein Listeria monocytogenes
4.99.1.9 R29L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 R45L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 S53A site-directed mutagenesis, the mutant shows altered ligand binding and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 T14V site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 T14V/Y46F/S53A site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 Y124F site-directed mutagenesis, the mutant variant shows the presence of a minor six coordinated low spin (6cLS) species in addition to the 5cHS form, the mutant shows altered ligand binding and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 Y124F site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
4.99.1.9 Y46F site-directed mutagenesis, the mutant shows altered ligand binding and thermostability compared to wild-type enzyme Listeria monocytogenes

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.99.1.9 additional information
-
 additional information steady-state kinetics of wild-type and mutant enzymes, overview Listeria monocytogenes

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.99.1.9 coproporphyrin III + Fe2+ Listeria monocytogenes
-
 Fe-coproporphyrin III + 2 H+
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.99.1.9 Listeria monocytogenes A0A5D5VUB4
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.99.1.9 coproporphyrin III + Fe2+
-
 Listeria monocytogenes Fe-coproporphyrin III + 2 H+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.99.1.9 CpfC
-
 Listeria monocytogenes

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.99.1.9 additional information
-
 additional information ligand kon rates, overview Listeria monocytogenes

Cofactor

EC Number Cofactor Comment Organism Structure
4.99.1.9 [2Fe-2S]-center the enzyme has a C-terminal [2Fe-2S] cluster Listeria monocytogenes

General Information

EC Number General Information Comment Organism
4.99.1.9 metabolism coproporphyrin ferrochelatase (CpfC) catalyses the insertion of ferrous iron into the porphyrin ring as the penultimate step within the coproporphyrin-dependent heme biosynthesis pathway. In the protoporphyrin-dependent (PPD) heme biosynthesis pathway, the protoporphyrin ferrochelatase (PpfC) is active, whereas in the coproporphyrin-dependent (CPD) heme biosynthesis pathway, coproporphyrin ferrochelatase (CpfC) is present, enzyme structure comparisons. CPD heme biosynthesis pathway starting from coproporphyrinogen III, overview Listeria monocytogenes
4.99.1.9 additional information analysis of the interactions of the four-propionate substrate, coproporphyrin III, and the fourpropionate product, iron coproporphyrin III (coproheme), with the CpfC from Listeria monocytogenes, differences with respect to the protoporphyrin IX and heme b complexes in the different CpfC enzymes, ligand binding structures, overview. Tyrosine Y124 in LmCpfC coordinates the propionate at position 2, which is conserved in monoderm CpfCs and is highly important for binding and stabilisation. A tyrosine-serine-threonine triad coordinates the propionate at position 4 Listeria monocytogenes
4.99.1.9 physiological function coproporpyhrin III is the substrate of coproporphyrin ferrochelatases (CpfCs). These enzymes catalyse the insertion of ferrous iron into the porphyrin ring. This is the penultimate step within the coproporphyrin-dependent heme biosynthesis pathway. In the CPD pathway, CpfC produces iron coproporphyrin III (coproheme), which is the substrate for coproheme decarboxylase (ChdC) Listeria monocytogenes