Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the proximal residue histidine 25 plays a key role in HO-1 activity | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
710-bp fragment encoded amino acids of wild-type and mutant HO-1 constructed in the plasmids pET28b(+)-hHO-1(w) and (m), expressed in Escherichia coli BL21 (DE3) | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
wild-type and mutant H25A, by hanging drop vapor diffusion method, at 2.8 A resolution. Mutant heme-HO-1 crystal is monoclinic, space group P21, there are four molecules in an asymmetric unit cell. The molecular surfaces of wild-type and mutant are of little difference, though the active pocket in the mutant is larger. The two have the same substrate affinity in electrostatic potential. A positive charge region on the edge of heme forms around the catalytic reaction pocket. After mutation, Ala is still located in the surface and does not influence the electrostatic potential of the reaction pocket | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
H25A | mutation leads to an empty pocket underneath the ferric ion in the heme, leading to loss of binding iron ligand. Enzymatic activity is reduced by 90.5%. By supplementing imidazole, the HO-1 activity is restored approximately 87.5% to its normal level | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | - |
Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
28000 | - |
x * 28000, wild-type and mutant, SDS-PAGE | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
on Ni-NTA column, wild-type 32fold purified and mutant H25A 31fold purified, more than 95% pure | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + electron donor + O2 | - |
Homo sapiens | biliverdin + Fe2+ + CO + oxidized electron donor + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 28000, wild-type and mutant, SDS-PAGE | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
heme oxygenase-1 | - |
Homo sapiens |
HO-1 | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Homo sapiens |