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Literature summary extracted from
- X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors (2008), J. Med. Chem., 51, 5943-5952.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.18 | truncated, soluble version of HO-1 that contains 233 amino acids expressed from plasmid HO1-t233/pBace in Escherichia coli DH5alpha | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.18 | HO-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone, by sitting-drop vapor diffusion method, at room temperature, to 1.5 A resolution. Overall structure of the HO-1-inhibitor complex is very similar to that of the native heme-conjugated HO-1, being mostly alpha-helical with the heme sandwiched between the proximal and distal helices. The inhibitor binds to the HO-1 distal pocket such that the imidazolyl moiety coordinates with heme iron while the adamantyl group is stabilized by a hydrophobic binding pocket. Distal helix flexibility, coupled with shifts in proximal residues and heme, acts to expand the distal pocket, thus accommodating the bulky inhibitor without displacing heme. Inhibitor binding effectively displaces the catalytically critical distal water ligand | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.18 | 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone | - |
Homo sapiens |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.18 | Fe2+ | - |
Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.18 | Homo sapiens | P09601 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.18 | on anion-exchange column | Homo sapiens |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.18 | heme + electron donor + O2 | - |
Homo sapiens | biliverdin + Fe2+ + CO + oxidized electron donor + H2O | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.14.18 | heme oxygenase-1 | - |
Homo sapiens |
| 1.14.14.18 | HO-1 | - |
Homo sapiens |
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