EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
second reductive step of the mechanism of interaction and electron transfer, overview |
Pseudomonas putida |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
wild-type dioxygen complex structure: high occupancy and a ordered structure of the iron-linked dioxygen and two 'catalytic' water molecules that form part of a proton relay system to the iron-linked dioxygen, Thr252 accepts a hydrogen bond from the hydroperoxy (Fe(III)-OOH) intermediate that promotes the second protonation on the distal oxygen atom, leading to O-O bond cleavage and compound I formation |
Pseudomonas putida |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
wild-type enzyme, but not mutant T252A |
Pseudomonas putida |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
CYP101D1, CYP101D2 |
Novosphingobium aromaticivorans |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
the reduced enzyme exhibits lower-amplitude motions of secondary structural features than the oxidized enzyme on all of the time scales accessible, and these differences are more pronounced in regions of the enzyme involved in substrate access to the active site (B' helix and beta3 and beta5 sheets) and binding of putidaredoxin (C and L helices), the iron-sulfur protein that acts as the effector and reductant of CYP101 in vivo |
Pseudomonas putida |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
though the active site of the enzyme resides deep inside the protein matrix, the substrate is recognized at the surface of the enzyme and directed towards the active site through the access channel. The threonine 192 that resides on the F-G loop and directed towards the putative substrate access channel of the enzyme, plays an important role in recognition of the substrate at the surface of the enzyme |
Pseudomonas putida |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
CYP101D1, CYP101D2 |
Novosphingobium aromaticivorans ATCC 700278D-5 |
(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
- |
Pseudomonas putida |
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
conformational change in CYP101 upon binding of putidaredoxin that re-orients bound camphor appropriately for hydroxylation |
Pseudomonas putida |
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
| 1.14.15.1 | (+)-camphor + O2 + reduced putidaredoxin |
ferric hydroperoxo complex, elusive reactive species of cytochrome P450cam, and the hydroxo intermediate (formed during camphor hydroxylation) in the catalytic cycle of cytochrome P450cam all have a doublet ground state which have a pronounced multiconfigurational character in the case of compound I and the hydroxo intermediate |
Pseudomonas putida |
exo-5-hydroxycamphor + oxidized putidaredoxin + H2O |
- |
? |
