Cloned (Comment) | Organism |
---|---|
expression of GST-tagged full-length HO-1 mutant R254K and of GST-tagged wild-type enzyme in Escherichia coli strain DH5alpha | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
R254K | site-directed mutagenesis, the exchange eliminates a thrombin cleavage site in the full-length enzyme, the mutant enzyme shows similar activity compared to the wild-type enzyme | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum | - |
Homo sapiens | 5783 | - |
membrane | - |
Homo sapiens | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32000 | - |
x * 32000, recombinant mutant R254K, SDS-PAGE | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + AH2 + O2 | Homo sapiens | HO-1 is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase, CPR, releasing free iron and carbon monoxide | biliverdin + Fe2+ + CO + A + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09601 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | HO-1 contains several thrombin cleavage sites, one of which is located at the C-terminus to cleave the membrane binding domain, overview | Homo sapiens |
Purification (Comment) | Organism |
---|---|
recombinant GST-tagged full-length HO-1 mutant R254K 54fold and recombinant wild-type enzyme 40fold by thrombin treatment and glutathione affinity chromatography, elution with 1.0% sarkosyl detergent and 2% octyl glucoside, the recombinant wild-type full-length enzyme is not stable during expression and purification due to proteolytic cleavage, overview | Homo sapiens |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0705 | - |
purified recombinant wild-type enzyme | Homo sapiens |
0.101 | - |
purified recombinant HO-1 mutant R254K | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
heme + AH2 + O2 | HO-1 is the chief regulatory enzyme in the oxidative degradation of heme to biliverdin. HO-1 receives the electrons necessary for catalysis from the flavoprotein NADPH cytochrome P450 reductase, CPR, releasing free iron and carbon monoxide | Homo sapiens | biliverdin + Fe2+ + CO + A + H2O | - |
? | |
heme + AH2 + O2 | the C-terminal 23 amino acids are essential for maximal catalytic activity | Homo sapiens | biliverdin + Fe2+ + CO + A + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 32000, recombinant mutant R254K, SDS-PAGE | Homo sapiens |
More | the C-terminal 23 amino acids are essential for maximal catalytic activity | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
heme oxygenase-1 | - |
Homo sapiens |
HO-1 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |