EC Number   |
Reaction |
Reference |
|---|
    1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
reaction mechanism |
674438 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
reaction mechanism and cycle of the enzyme including postulated intermediates, detailed overview |
674516 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
reaction mechanism involving a heme ring and residue Asp297, modelling of the hydroxylation of camphor and the hydrogen abstraction from heme using combined quantum mechanical/molecular mechanical method |
676280 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
reaction mechanism, and second reductive step of the mechanism of interaction and electron transfer, overview |
672070 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
rebound mechanism of C-H hydroxylation by P450, molecular dynamics |
674197 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
the active site structure changes due to putidaredoxin-enzyme interaction involving salt bridge and hydrogen bonding network between Arg112, His355, Leu356, and the heme ligand Cys357 |
672413 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
the acvtive conformation of enzyme is stabilized by binding of the substrate at the active site |
659528 |
| 1.14.15.1 | (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
via H2O2 and a nucleophilic intermediate, the substrate can modulate the properties of both the monoxygenase active-oxygen intermediates and the proton-delivery network that encompasses them, the catalytic cycle, overview |
674152 |
