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Results 1 - 10 of 19 > >>
EC Number
Reaction
Commentary
Reference
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
active binding of substrate camphor, analysis by density functional theory calculations, residue Tyr96 is important forming a strong hydrogen bond, catalytic cycle of cytochrome P450, the strong hydrogen bonding is not affected by the enzyme's environment, reaction mechanism, overview
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
binding of putidaredoxin forces selection of the active conformation of enzyme
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
K+ plays an important role in substrate binding and structural and conformational stability of the enzyme
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
mechanism of O2 activation: binding of O2 to ferrous P450cam to yield the ferric-superoxo form, oxyP450cam, followed by an irreversible, long-range electron transfer from putidaredoxin to reduce the oxyP450cam, camphor is bound to all enzyme forms, overview
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
model for putidaredoxin activity, primary role of putidaredoxin is to prevent uncoupling by enforcing conformations of enzyme that prevent loss of substrate and to enforce conformations that permit efficient proton transfer
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
multi-component mixed function oxidase, consisting of putidaredoxin reductase, putidaredoxin and cytochrome P450cam, heme-thiolate protein
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
oxygen-transfer reaction via a monooxygenation mechanism
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
proposed catalytic cycle for cytochrome P450, a ferryl-oxo Pi-cation porphyrin radical, is the putative oxidant that reacts directly with substrate, overview. The axial ligand to the heme iron, a cysteine thiolate, is generally believed to control P450 reactivity
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
proposed catalytic cycle for cytochrome P450, a ferryl-oxo Pi-cation porphyrin radical, is the putative oxidant that reacts directly with substrate, overview. The axial ligand to the heme iron, a cysteine thiolate, is generally believed to control P450 reactivity; proposed catalytic cycle for cytochrome P450, overview
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
proposed catalytic cycle for cytochrome P450, overview
Results 1 - 10 of 19 > >>