EC Number   |
General Information |
Reference |
|---|
    1.14.15.1 | evolution |
cytochrome P450cam (CYP101) from Pseudomonas putida is the model enzyme for the P450 superfamily |
744192 |
| 1.14.15.1 | evolution |
the enzyme belongs to the superfamily of cytochrome P450 monooxygenases |
725873 |
| 1.14.15.1 | malfunction |
alanine substitutions of the residues involved in putidaredoxin-enzyme interactions do not influence the rates of electron transfer, interaction analysis of enzyme wild-type and mutant (D125A, H352A, and H361A) proteins with putidaredoxxin wild-type and mutant (Y33A, S42A, and S44A) proteins, kinetics, overview |
744698 |
| 1.14.15.1 | malfunction |
structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine, mapping of the effects of the sulfur-to-selenium substitution on the individual steps of the catalytic cycle. The more electron-donating selenolate ligand has only negligible effects on substrate, product, and oxygen binding, electron transfer, catalytic turnover, and coupling efficiency. Off-pathway reduction of oxygen to give superoxide is the only step significantly affected by the mutation. Incorporation of selenium accelerates this uncoupling reaction approximately 50fold compared to sulfur, but because the second electron transfer step is much faster, the impact on overall catalytic turnover is minimal. Quantum mechanical calculations, Lewis structure of our P450cam active site model and quantum mechanically optimized structures (with TPSS/SVP) of the oxygen-bound forms with S and Se in the triplet spin state, overview |
-, 744343 |
| 1.14.15.1 | metabolism |
camphor binding results in a low-spin to high-spin spectral change. The high-spin transition in P450cam occurs immediately upon camphor addition but is very slow with a half-life of 25 min. Association of camphor shows a DELTAH of <0. The product molecule can occupy two different orientations |
764173 |
| 1.14.15.1 | metabolism |
putidaredoxin binds to a state of P450cam, where the substrate entry channel is partially open, the active site residues are positioned to facilitate the formation of a water-mediated proton relay network akin to those observed for the open state. The formation of this conformation is driven by binding of an allosteric camphor molecule prior to the first electron transfer step. Upon binding, the R186-D251 salt bridge is destabilized and breaks, allowing partial opening of the substrate entry channel and forming a conformation favorable to putidaredoxin binding. Putidaredoxin stabilizes this conformation during both electron transfer steps and keeps the R186-D251 bridge broken so a water-mediated proton relay network can form. Following the second electron transfer step, putidaredoxin remains in complex with P450cam and helps to promote the opening of channel 2 |
764184 |
| 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 |
cofactor putidaredxin-bound and substrate-bound wild-type and E195C/A199C mutant enzymes, camphor-free, cyanide-bound P450cam, and apoenzyme structure analysis, structure analysis using crystal structure, PDB IDs 4JWS and 3L63. Cyanide and camphor can bind simultaneously in the active site |
746306 |
| 1.14.15.1 | more |
CYP101A1 is a soluble monomeric heme-containing camphor monooxygenase |
711268 |
| 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 |
