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Literature summary for 1.14.14.18 extracted from

  • Huber, W.J.; Backes, W.L.
    Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase (2007), Biochemistry, 46, 12212-12219.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

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

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
Homo sapiens 5783
-
membrane
-
Homo sapiens 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, recombinant mutant R254K, SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Homo sapiens P09601
-
-

Posttranslational Modification

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 (Commentary)

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 [micromol/min/mg]

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 and Products (Substrate)

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

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

Synonyms Comment Organism
heme oxygenase-1
-
Homo sapiens
HO-1
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens