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Literature summary for 1.14.14.18 extracted from
- Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism (2005), J. Biol. Chem., 280, 2981-2989.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| wild-type and mutants D136E, D136N, D136A, D136F | Corynebacterium diphtheriae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D136A | reduced heme degradation activity, formation of ferryl heme | Corynebacterium diphtheriae |
| D136E | enzymic activity similar to wild-type | Corynebacterium diphtheriae |
| D136F | reduced heme degradation activity, formation of ferryl heme | Corynebacterium diphtheriae |
| D136N | enzymic activity similar to wild-type | Corynebacterium diphtheriae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium diphtheriae | P71119 | - |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O | model of activation mechanism of Fe-OOH | Corynebacterium diphtheriae |
aSynonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HmuO | - |
Corynebacterium diphtheriae |
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