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Literature summary for 4.99.1.9 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
Search for more literature for 4.99.1.9

Protein Variants

Protein Variants Comment Organism
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
R29L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
R45L site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
S53A site-directed mutagenesis, the mutant shows altered ligand binding and thermostability compared to wild-type enzyme Listeria monocytogenes
T14V site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
T14V/Y46F/S53A site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
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
Y124F site-directed mutagenesis, the mutant shows altered ligand binding, kinetics, and thermostability compared to wild-type enzyme Listeria monocytogenes
Y46F site-directed mutagenesis, the mutant shows altered ligand binding and thermostability compared to wild-type enzyme Listeria monocytogenes

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Listeria monocytogenes A0A5D5VUB4
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
CpfC
-
 Listeria monocytogenes

Turnover Number [1/s]

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

Cofactor

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

General Information

General Information Comment Organism
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
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
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