Literature summary for 1.14.15.1 extracted from

Skinner, S.P.; Follmer, A.H.; Ubbink, M.; Poulos, T.L.; Houwing-Duistermaat, J.J.; Paci, E.
Partial opening of cytochrome P450cam (CYP101A1) is driven by allostery and putidaredoxin binding (2021), Biochemistry, 60, 2932-2942 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
cyanide	binding of cyanide results in significant conformational changes and two different rotamers for residue D251	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P00183	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(+)-camphor + reduced putidaredoxin + O2	-	Pseudomonas putida	(+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O	-	?

Synonyms

Synonyms	Comment	Organism
P450cam	-	Pseudomonas putida

General Information

General Information	Comment	Organism
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	Pseudomonas putida

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Release 2023.1 (January 2023)