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Literature summary for 1.14.14.18 extracted from

  • Wilks, A.; Schmitt, M.P.
    Expression and characterization of a heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Iron acquisition requires oxidative cleavage of the heme macrocyle (1998), J. Biol. Chem., 273, 837-841.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and His-tagged enzyme in Escherichia coli Corynebacterium diphtheriae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
x * 25000, recombinant enzyme, SDS-PAGE Corynebacterium diphtheriae

Organism

Organism UniProt Comment Textmining
Corynebacterium diphtheriae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and His-tagged enzyme, ion-exchange, gel filtration Corynebacterium diphtheriae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
heme + electron donor + O2 electron donor NADPH, reductase: human or E. coli NADPH-cytochrome P450 reductase or putidaredoxin/putidaredoxin reductase Corynebacterium diphtheriae biliverdin + Fe2+ + CO + oxidized eletron donor + H2O
-
?

Subunits

Subunits Comment Organism
? x * 25000, recombinant enzyme, SDS-PAGE Corynebacterium diphtheriae