Ferrochelatase is the final enzyme in the heme biosynthetic pathway. It plays a critical role by converting protoporphyrin IX into heme by inserting ferrous iron. In bacteria like Enterococcus faecalis, which do not synthesize heme de novo, ferrochelatase can utilize exogenous protoporphyrin IX to produce heme for hemoproteins .
While specific studies on recombinant Enterococcus faecalis ferrochelatase (hemH) are scarce, the enzyme's role in utilizing protoporphyrin IX to produce heme is crucial for the bacterium's ability to form hemoproteins. This capability allows Enterococcus faecalis to adapt to environments where heme is not readily available.
| Feature | Description |
|---|---|
| Function | Inserts ferrous iron into protoporphyrin IX to form heme. |
| Role in E. faecalis | Utilizes exogenous protoporphyrin IX to produce heme for hemoproteins. |
| Potential Applications | Biotechnological production of heme-containing compounds. |
Bryan-Jones, D. G., & Whittenbury, R. (1969). Hemoprotein synthesis by bacteria. Journal of General Microbiology, 58(3), 247-260.
Frankenberg, L. (n.d.). Hemoproteins of Enterococcus faecalis. Lucris.
Saillant, et al. (2021). A Novel Enterococcus faecalis Heme Transport Regulator (FhtR). PMC.
Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III, forming Fe-coproporphyrin III.
KEGG: efa:EF1989
STRING: 226185.EF1989