EC Number   |
General Information |
Reference  |
|---|
    1.14.15.1 | more |
CYP101A1 is a soluble monomeric heme-containing camphor monooxygenase |
711268 |
| 1.14.15.1 | more |
role of Tyr96 in substrate binding |
724082 |
| 1.14.15.1 | more |
both the apoenzyme and the camphor-bound enzyme of CYP101D2 have open conformations with an access channel. In the active site of the camphor-bound form, the camphor carbonyl interacts with the heme-iron-bound water. The observed open structures may be conformers of the CYP101D2 enzyme that enable the substrate to enter the buried active site via a conformational selection mechanism. Two other potential camphor-binding sites exist: one located in the access channel, flanked by the B/C and F/G loops and the I helix, and the other in a cavity on the surface of the enzyme near the F helix side of the F/G loop. The second and third binding sites may be intermediate locations of substrate entry and translocation into the active site, substrate binding structure and multi-step substrate-binding mechanism, overview |
-, 724221 |
| 1.14.15.1 | more |
NMR structure analysis of the enzyme CYP101A1 with substrate (+)-camphor bound the active site and substrate-free enzyme after removal of (+)-camphor, molecular dynamics simulations and modeling, overview. Portions of a beta-rich region adjacent to the active site shift so as to partially occupy the vacancy left by removal of substrate. The accessible volume of the active site is reduced in the substrate-free enzyme relative to the substrate-bound structure |
724338 |
| 1.14.15.1 | more |
P450cam from Pseudomonas putida oxidizes (1R)-(+)-camphor to 5-exo-hydroxy camphor and further to 5-oxo-camphor |
-, 725602 |
| 1.14.15.1 | physiological function |
Pseudomonas putida is capable of detoxification of camphor and borneol, overview |
-, 725602 |
| 1.14.15.1 | evolution |
the enzyme belongs to the superfamily of cytochrome P450 monooxygenases |
725873 |
| 1.14.15.1 | more |
substrate recognition and selectivity, enzyme-substrate interactions, NMR structrue analysis, Analysis of 1H,15N-TROSY-HSQC spectra of CYP-(+)-camphor-CO, CYP-adamantenone-CO and CYP-norcamphor-CO. overview. Replacing the native substrate camphor with adamantanone or norcamphor causes perturbations in NMR-detected NH correlations assigned to the network,which includes portions of a beta-sheet and an adjacent helix that is remote from the active site |
725873 |
| 1.14.15.1 | evolution |
cytochrome P450cam (CYP101) from Pseudomonas putida is the model enzyme for the P450 superfamily |
744192 |
| 1.14.15.1 | more |
double electron-electron resonance measurements of intermolecular distances in the Pdx/P450cam complex show that the geometry of the complex is nearly identical for the open and closed states of P450cam |
744192 |
