EC Number   |
Title |
Organism |
|---|
  4.99.1.9 | Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III propionate interactions and porphyrin core deformation |
Listeria monocytogenes |
| 4.99.1.9 | Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX |
Bacillus subtilis |
| 4.99.1.9 | Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX |
Bacillus subtilis 168 |
| 4.99.1.9 | Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes |
Bacillus subtilis |
| 4.99.1.9 | Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes |
Bacillus subtilis 168 |
| 4.99.1.9 | Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis |
Bacillus subtilis |
| 4.99.1.9 | Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis |
Bacillus subtilis 168 |
| 4.99.1.9 | Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase |
Listeria monocytogenes |
| 4.99.1.9 | Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin |
Bacillus subtilis |
| 4.99.1.9 | Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin |
Cutibacterium acnes |
