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Literature summary for 1.14.14.18 extracted from

  • Chu, G.C.; Katakura, K.; Zhang, X.; Yoshida, T.; Ikeda-Saito, M.
    Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae (1999), J. Biol. Chem., 274, 21319-21325.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Corynebacterium diphtheriae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24000
-
x * 24000, SDS-PAGE, deduced from amino acid sequence Corynebacterium diphtheriae

Organism

Organism UniProt Comment Textmining
Corynebacterium diphtheriae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Corynebacterium diphtheriae

Reaction

Reaction Comment Organism Reaction ID
protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O a ferric hydroperoxide species must be an active intermediate in the first oxygenation step Corynebacterium diphtheriae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + electron donor + O2 electron donor ascorbic acid Corynebacterium diphtheriae biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
?

Subunits

Subunits Comment Organism
? x * 24000, SDS-PAGE, deduced from amino acid sequence Corynebacterium diphtheriae