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Literature summary for 1.14.14.18 extracted from

  • Wilks, A.; de Montellano, P.R.O.; Sun, J.; Loehr, T.M.
    Heme oxygenase (HO-1): His-132 stabilizes a distal water ligand and assists catalysis (1996), Biochemistry, 35, 930-936.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
H132A heme oxygenase-1, 40-50% of wild-type activity Homo sapiens
H132G heme oxygenase-1, 40-50% of wild-type activity Homo sapiens
H132S heme oxygenase-1, 20% of wild-type activity Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.003
-
heme heme oxygenase-1, wild-type Homo sapiens
0.014
-
heme heme oxygenase-1, H132G and H132A mutants Homo sapiens
0.018
-
heme heme oxygenase-1, H132S mutant Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + electron donor + O2
-
Homo sapiens biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
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