CATH Classification
Level | CATH Code | Description |
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1 | Mainly Alpha |
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1.20 | Up-down Bundle |
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1.20.910 | Heme Oxygenase; Chain A |
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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 P30519
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)
P30519 |
HMOX2_HUMAN
Homo sapiens
Heme oxygenase 2
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PDB Structure
PDB | 2Q32 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Comparison of Apo- and Heme-bound Crystal Structures of a Truncated Human Heme Oxygenase-2.
J.Biol.Chem.
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