EC Number   |
General Information |
Reference |
|---|
   1.14.99.15 | evolution |
the enzyme belongs to the superfamily of heme-dependent cytochrome P450 monooxygenases |
-, 727349 |
| 1.14.99.15 | more |
substrate-enzyme structure, the enzyme possesses a clearly defined substrate access channel that is formed between the BC loop and the G and G' helices, overview. The 4-methoxybenzoate-bound enzyme has a closed conformation, in contrast to the substrate-free form of CYP199A2 where an obvious substrate access channel is observed. The switch from an open to a closed conformation arises from pronounced residue side-chain movements and alterations of ion pair and hydrogen bonding interactions at the entrance of the access channel. A chloride ion bound just inside the protein surface caps the entrance to the active site and protects the substrate and the heme from the external solvent. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate |
-, 727349 |
| 1.14.99.15 | more |
the 4-methoxybenzoate-bound enzyme has a closed conformation. The substrate is held in place via hydrophobic and hydrogen bond interactions. The methoxy group is located over the heme iron, accounting for the high activity and selectivity of the enzyme for oxidative demethylation of 4-methoxybenzoate, involvement of hydrophobic (Phe185) and hydrophilic (Arg92, Ser95 and Arg243) amino acid residues in the binding of para-substituted benzoates |
-, 727349 |
| 1.14.99.15 | physiological function |
CYP199A2 catalyzes the oxidative demethylation of 4-methoxybenzoic acid and the hydroxylation and desaturation of 4-ethylbenzoic acid, and thus may play a role in lignin degradation by this organism |
-, 699026 |
| 1.14.99.15 | physiological function |
CYP199A2 is involved in the degradation of ligninolic compounds by the organism |
-, 727349 |
