Heme oxygenase
| heme oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Heme oxygenase I, homodimer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 1.14.99.3 | ||||||||
| CAS no. | 9059-22-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Heme oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Crystal structures of ferrous and ferrous-no forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage | |||||||||
| Identifiers | |||||||||
| Symbol | Heme_oxygenase | ||||||||
| Pfam | PF01126 | ||||||||
| Pfam clan | CL0230 | ||||||||
| InterPro | IPR016053 | ||||||||
| PROSITE | PDOC00512 | ||||||||
| SCOP2 | 1qq8 / SCOPe / SUPFAM | ||||||||
| Membranome | 532 | ||||||||
| |||||||||
Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous iron, and carbon monoxide.[1]
There are many heme degrading enzymes in nature. In general, only aerobic heme degrading enzymes are referred to as HMOX-like enzymes whereas anaerobic enzymes are typically not affiliated with the HMOX family.
- ^ Ryter SW, Alam J, Choi AM (April 2006). "Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications". Physiological Reviews. 86 (2): 583–650. doi:10.1152/physrev.00011.2005. PMID 16601269.