Literature summary for 1.14.15.1 extracted from

Sakurai, K.; Shimada, H.; Hayashi, T.; Tsukihara, T.
Substrate binding induces structural changes in cytochrome P450cam (2009), Acta Crystallogr. Sect. F, 65, 80-83.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli strain JM109	Pseudomonas putida

Crystallization (Commentary)

Crystallization (Comment)	Organism
two ferric P450cam structures partially complexed with (+)-camphor, by sitting-drop vapour-diffusion method, at 1.3 A (soaked crystals) or 1.35 A (unsoaked crystals) resolution. Belongs to space group P43212, unsoaked crystals have unit-cell parameters of a = b = 63.38, c = 247.30, whereas soaked crystals have unit-cell parameters of a = b = 63.61 and c = 250.39. Structure of the unsoaked P450cam shows an active site that is partially occupied by (+)-camphor and a water molecule liganded to the haem iron and rotamers of Thr101. (+)-Camphor-bound form is the major component and the water-bound form is the minor component. In the soaked P450cam, the population of the major component increases, while the minor component decreases. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to redox-potential change	Pseudomonas putida

Crystallization (Comment)

Organism

two ferric P450cam structures partially complexed with (+)-camphor, by sitting-drop vapour-diffusion method, at 1.3 A (soaked crystals) or 1.35 A (unsoaked crystals) resolution. Belongs to space group P43212, unsoaked crystals have unit-cell parameters of a = b = 63.38, c = 247.30, whereas soaked crystals have unit-cell parameters of a = b = 63.61 and c = 250.39. Structure of the unsoaked P450cam shows an active site that is partially occupied by (+)-camphor and a water molecule liganded to the haem iron and rotamers of Thr101. (+)-Camphor-bound form is the major component and the water-bound form is the minor component. In the soaked P450cam, the population of the major component increases, while the minor component decreases. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to redox-potential change

Pseudomonas putida

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	-	Pseudomonas putida

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	P00183	-	-

Purification (Commentary)

Purification (Comment)	Organism
to homogeneity by SDSPAGE	Pseudomonas putida

Storage Stability

Storage Stability	Organism
-80°C, 50 mM potassium phosphate buffer, pH 7.4, 50 mM KCl, 1 mM (+)-camphor	Pseudomonas putida

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
cytochrome p450cam	-	Pseudomonas putida
P450cam	-	Pseudomonas putida

Cofactor

Cofactor	Comment	Organism	Structure
putidaredoxin	-	Pseudomonas putida