CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.910 | Heme Oxygenase; Chain A |
|
1.20.910.10 | Heme oxygenase-like |
Domain Context
CATH Clusters
| Superfamily | Heme oxygenase-like |
| Functional Family | Heme oxygenase 1 |
Enzyme Information
| 1.14.14.18 |
Heme oxygenase (biliverdin-producing).
based on mapping to UniProt P09601
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.
-!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3.
|
UniProtKB Entries (1)
| P09601 |
HMOX1_HUMAN
Homo sapiens
Heme oxygenase 1
|
PDB Structure
| PDB | 1TWR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage.
J.Inorg.Biochem.
|
