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Literature summary extracted from

  • Hofbauer, S.; Helm, J.; Obinger, C.; Djinovic-Carugo, K.; Furtmueller, P.G.
    Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase (2020), FEBS J., 287, 2779-2796.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.99.1.9 gene cpfC, sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli Listeria monocytogenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.99.1.9 purified recombinant His-tagged enzyme in apoform and with bound product coproheme, mixing of 9.5 mg/ml protein with or without bound ligand in solution with 16% w/v PEG 8000, 20% v/v glycerol, and 0.04 M KH2PO4 for the apo-enzyme crystals and with 0.1 M Bis-Tris, pH 5.5, 25% PEG 3350, 0.2 M MgCl2 for the complexed enzyme, 2 days, X-ray diffraction structure determination and analysis, molecular replacement using the PDB structure 2HK6 of BsCpfC enzyme as template 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 Michaelis-Menten kinetics Listeria monocytogenes
4.99.1.9 0.00028
-
 Fe2+ pH 7.0, 25°C, recombinant enzyme 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
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.99.1.9 recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and desalting gel filtration Listeria monocytogenes

Renatured (Commentary)

EC Number Renatured (Comment) Organism
4.99.1.9 reconstitution of LmCpfC for crystallization with coproheme is performed by the addition of a 1.2 fold molar excess, and the complex is purified by gel filtration Listeria monocytogenes

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+
-
 ?
4.99.1.9 coproporphyrin III + Fe2+ the reaction is carried out anaerobically under argon flow and in the dark Listeria monocytogenes Fe-coproporphyrin III + 2 H+
-
 ?
4.99.1.9 additional information when LmCpfC is incubated with both substrates, Fe2+ and coproporphyrin III, Fe-coproporphyrin III (coproheme) is the only detected species Listeria monocytogenes ?
-
-

Synonyms

EC Number Synonyms Comment Organism
4.99.1.9 CpfC
-
 Listeria monocytogenes
4.99.1.9 ferrochelatase
-
 Listeria monocytogenes
4.99.1.9 LmCpfC
-
 Listeria monocytogenes

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.99.1.9 25
-
 assay at Listeria monocytogenes

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.99.1.9 additional information
-
 binding of coproporphyrin III or coproheme to apo-LmCpfC has a strong stabilizing effect on the protein, as reflected in the increased thermal stability of the resulting complexes 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 0.132
-
 Fe2+ pH 7.0, 25°C, recombinant enzyme Listeria monocytogenes

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.99.1.9 7
-
 assay at Listeria monocytogenes

General Information

EC Number General Information Comment Organism
4.99.1.9 evolution phylogenetic analysis Listeria monocytogenes
4.99.1.9 metabolism coproporphyrin ferrochelatases (CpfCs) insert ferrous iron into coproporphyrin III yielding coproheme. CpfCs are utilized by prokaryotic, mainly monoderm (Gram-positive) bacteria within the coproporphyrin-dependent (CPD) heme biosynthesis pathway Listeria monocytogenes
4.99.1.9 additional information analysis of the catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase, crystal structures analysis and calorimetric methods, detailed overview. UV-vis absorption spectroscopy of LmCpfC with the substrate coproporphyrin III and the product coproheme, spectral transitions upon binding of coproporphyrin III to apo-LmCpfC shows a biphasic behavior, structure comparisons. Binding of coproporphyrin III or coproheme to apo-LmCpfC has a strong stabilizing effect on the protein, as reflected in the increased thermal stability of the resulting complexes Listeria monocytogenes
4.99.1.9 physiological function coproporphyrin ferrochelatases (CpfCs) insert ferrous iron into coproporphyrin III yielding coproheme. CpfCs are utilized by prokaryotic, mainly monoderm (Gram-positive) bacteria within the coproporphyrin-dependent (CPD) heme biosynthesis pathway Listeria monocytogenes