EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.14.18 | additional information | C-terminal truncation of the enzyme, e.g. by sequential deletion of three residues, His207, Arg208, His209. Deleting His209 minimally perturbs the interaction of the C-terminus, but deletion of Arg208 completely abolishes it | Neisseria meningitidis |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.14.14.18 | azide | - |
Neisseria meningitidis | |
1.14.14.18 | cyanide | - |
Neisseria meningitidis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.14.18 | Neisseria meningitidis | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.14.18 | protoheme + 3 [reduced NADPH-hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH-hemoprotein reductase] + 3 H2O | heme degradation by heme oxygenase proceeds through three successive steps of O2 activation. The first step is formation of alpha-meso-hydroxyheme from from heme, second formation of verdoheme from alpha-meso-hydroxyheme, the third step is the ring opening of alpha-verdoheme to alpha-biliverdin, overview | Neisseria meningitidis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.14.14.18 | additional information | the enzyme shows substrate-protein, specifically pyrrole-I/II-helix-2, peripheral interactions. The enzyme's C-terminus interacts with substrate in solution, interaction of the C-terminus with the active site destabilizes the crystallographic protohemin orientation, which is consistent with optimizing the His207-Asp27 H-bond, active site stress for product release, NMR analysis of wild-type and mutant enzymes, overview. Thermodynamics of substrate orientational isomerism are mapped for substrates with individual vinyl to methyl to hydrogen substitutions and with enzyme C-terminal deletions. Replacing bulky vinyls with hydrogens results in a 180 degree rotation of substrate about the alpha,gamma-meso axis in the active site | Neisseria meningitidis |