EC Number   |
General Information |
Reference |
|---|
  4.99.1.9 | evolution |
phylogenetic analysis |
771056 |
| 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 |
771075 |
| 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 |
771056 |
| 4.99.1.9 | metabolism |
the enzyme catalyzes the terminal step in heme biosynthesis |
-, 739725 |
| 4.99.1.9 | metabolism |
the enzyme participates in heme biosynthesis |
34963 |
| 4.99.1.9 | more |
active site architecture of wild-type and R45L mutant coproporphyrin ferrochelatases with bound physiological substrate coproporphyrin III, crystal structure analysis, propionate interactions and porphyrin core deformation, detailed overview. A cleft, build by structural elements of both ferredoxin-like domains, contains several conserved amino acid residues (distal H182 and E263, proximal Y12) and is the porphyrin binding site, where catalysis happens. The monomeric enzyme exhibits two ferredoxin-like domains, each with a four-stranded parallel beta-sheet flanked by alpha-helices. In cpIII-LmCpfC, as well as in the coproheme-bound structure, the porphyrin is oriented in the active site with the propionates 2 and 4 (p2 and p4) pointing to the inner core of the protein, p6 and p7 face towards the protein surface and are much more solvent exposed. In both cpIII and coproheme complexes with LmCpfC the H-bond interactions between the four propionates and six amino acids, Thr14, Arg29, Arg45, Tyr46, Ser53, and Tyr124, are fundamental to the porphyrin stabilization |
775669 |
| 4.99.1.9 | more |
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 |
771056 |
| 4.99.1.9 | more |
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 |
771075 |
| 4.99.1.9 | physiological function |
a hemH mutant primarily accumulates protoporphyrin IX |
-, 738499 |
| 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 |
771056 |
