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 P06762
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.
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UniProtKB Entries (1)
P06762 |
HMOX1_RAT
Rattus norvegicus
Heme oxygenase 1
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PDB Structure
PDB | 1IX4 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal Structures of Ferrous and CO-, CN(-)-, and NO-Bound Forms of Rat Heme Oxygenase-1 (HO-1) in Complex with Heme: Structural Implications for Discrimination between CO and O(2) in HO-1.
Biochemistry
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