EC Number | Activating Compound | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.18 | propionate | the enzyme requires only a single propionate interacting with the buried terminus of Lys16 to exhibit full activity, and it tolerates the existence of a propionate at the exposed 8-position | Neisseria meningitidis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.18 | azide | binding structure, NMR analysis, overview | Neisseria meningitidis | |
1.14.14.18 | cyanide | binding structure, NMR analysis, overview | Neisseria meningitidis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.18 | heme + 3 AH2 + 3 O2 | Neisseria meningitidis | - |
biliverdin + Fe2+ + CO + 3 A + 3 H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.18 | Neisseria meningitidis | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.14.18 | heme + 3 AH2 + 3 O2 | - |
Neisseria meningitidis | biliverdin + Fe2+ + CO + 3 A + 3 H2O | - |
? | |
1.14.14.18 | heme + 3 reduced ascorbate + 3 O2 | - |
Neisseria meningitidis | biliverdin + Fe2+ + CO + 3 oxidized ascorbate + 3 H2O | - |
? |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.18 | ascorbate | - |
Neisseria meningitidis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.14.18 | additional information | analysis of enzyme-protohemin substrate variant complexes and of enzyme-propionate substrate complexes by NMR, active site structure, overview. The enzyme's C-terminal fragment interacts with the active site of the enzyme. The C-terminal dipeptide Arg208-His209 cleaves spontaneously. Stronger hydrophobic contacts between pyrroles A and B with the enzyme contribute more substantially to the substrate binding free energy than in mammalian HOs, liberating one propionate to stabilize the C-terminus | Neisseria meningitidis |