EC Number   |
General Information |
Reference  |
|---|
  4.99.1.9 | metabolism |
the enzyme participates in heme biosynthesis |
34963 |
| 4.99.1.9 | physiological function |
hemH mutants accumulate all three tetrapyrroles: uroporphyrin, coproporphyrin, and protoporphyrin. Porphyrin accumulation does not occur in these mutants (in a hemA4 background) in the absence of 5-aminolevulinic acid |
738498 |
| 4.99.1.9 | physiological function |
a hemH mutant primarily accumulates protoporphyrin IX |
-, 738499 |
| 4.99.1.9 | metabolism |
the enzyme catalyzes the terminal step in heme biosynthesis |
-, 739725 |
| 4.99.1.9 | evolution |
phylogenetic analysis |
771056 |
| 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 | 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 | 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 |
| 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 | 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 |
