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Literature summary for 1.14.14.18 extracted from

  • Unno, M.; Ardevol, A.; Rovira, C.; Ikeda-Saito, M.
    Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation (2013), J. Biol. Chem., 288, 34443-34458.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Corynebacterium diphtheriae

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, free enzyme is crystallized by using 85 mM sodium cacodylate, pH 6.5, 25.5% (w/v) PEG8000, 170 mM sodium acetate, and 23.5% (v/v) glycerol, while substrate-bound enzyme is crystallized by using 50 mM MES, pH 6.1, 2.2 M ammonium sulfate, and 25% (w/v) sucrose, supplemented with 200 mM sodium ascorbate Corynebacterium diphtheriae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protoheme + [reduced NADPH-hemoprotein reductase] + O2 Corynebacterium diphtheriae
-
 biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium diphtheriae Q54AI1
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium diphtheriae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protoheme + [reduced NADPH-hemoprotein reductase] + O2
-
 Corynebacterium diphtheriae biliverdin + Fe2+ + CO + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

Synonyms Comment Organism
heme oxygenase
-
 Corynebacterium diphtheriae
HmuO
-
 Corynebacterium diphtheriae