Cloned (Comment) | Organism |
---|---|
overexpression of GST-tagged wild-type and mutant HO-2 in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Comment) | Organism |
---|---|
apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region, apo-HO-2: hanging drop method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 40% PEG 1500, 200 mM potassium glutamate, and 100 mM triethanolamine, pH 8.5, at 4°C, heme-bound HO-2: hanging drop vapour diffusion method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 33% PEG dimethlyether 500, 20 mM MgCl2, and 100 mM HEPES, pH 8.5, at 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution for the apoenzyme, and at 2.6 A resolution for the heme-bound enzyme | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + AH2 + O2 | Homo sapiens | first step in the heme degradation pathway | biliverdin + Fe2+ + CO + A + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P30519 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant GST-tagged wild-type and mutant HO-2 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + AH2 + O2 | first step in the heme degradation pathway | Homo sapiens | biliverdin + Fe2+ + CO + A + H2O | - |
? | |
heme + AH2 + O2 | proper orientation of heme in HO-2 is required for the regioselective oxidation of the alpha-mesocarbon. This is accomplished by interactions within the heme binding pocket, which is made up of two helices. The iron coordinating residue, His45, resides on the proximal helix. The distal helix contains highly conserved glycine residues that allow the helix to flex and interact with the bound heme. Tyr154, Lys199, and Arg203 orient the heme through direct interactions with the heme propionates, overview | Homo sapiens | biliverdin + Fe2+ + CO + A + H2O | - |
? | |
additional information | structure-function analysis | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structure-function analysis | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
heme oxygenase-2 | - |
Homo sapiens |
HO-2 | - |
Homo sapiens |