Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | - |
- |
- |
Synechocystis sp. | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
gamma-CH-Fe(cor) + 3 AH2 + 3 O2 | the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview | Arabidopsis thaliana | ? | - |
? | |
gamma-CH-Fe(cor) + 3 AH2 + 3 O2 | the regioisomeric iron corrole is an artificial, not-natural substrate, the enzymatic cleavage happens selectively at the unexpected bipyrrolic position and yields a biomimetic biliverdin-like product. The enzymatic corrole ring opening is selective for this corrole regioisomer and for plant-type heme oxygenase, mechanism, overview | Synechocystis sp. | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | heme oxygenases are widely distributed enzymes involved in the oxidative cleavage of the heme macrocycle that yields the open-chain tetrapyrrole biliverdin IX, CO, and iron | Arabidopsis thaliana |
physiological function | heme oxygenases are widely distributed enzymes involved in the oxidative cleavage of the heme macrocycle that yields the open-chain tetrapyrrole biliverdin IX, CO, and iron | Synechocystis sp. |