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Literature summary 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)

EC Number Cloned (Comment) Organism
1.14.14.18
-
 Corynebacterium diphtheriae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.14.18 24000
-
 x * 24000, SDS-PAGE, deduced from amino acid sequence Corynebacterium diphtheriae

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.18 Corynebacterium diphtheriae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.14.18
-
 Corynebacterium diphtheriae

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.14.18 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
a

Substrates and Products (Substrate)

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

Subunits

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