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Literature summary for 1.14.14.18 extracted from

  • Lad, L.; Koshkin, A.; de Montellano, P.R.; Poulos, T.L.
    Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity (2005), J. Biol. Inorg. Chem., 10, 138-146.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapour diffusion method Homo sapiens

Protein Variants

Protein Variants Comment Organism
G139A retains about 60% of the wild type HO activity Homo sapiens
G143H the replacement of Gly143 with His leads to the formation of a bis-histidine complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P09601
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-

Purification (Commentary)

Purification (Comment) Organism
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Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + 2 NADPH + 2 H+ + 2 O2
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Homo sapiens biliverdin + Fe2+ + CO + 2 NADP+ + H2O
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Synonyms

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