Literature summary for 1.14.15.1 extracted from

Kelly, P.; Eichler, A.; Herter, S.; Kranz, D.; Turner, N.; Flitsch, S.
Active site diversification of P450cam with indole generates catalysts for benzylic oxidation reactions (2015), Beilstein J. Org. Chem., 11, 1713-1720 .

Search for more literature for 1.14.15.1

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)	Pseudomonas putida

Protein Variants

Protein Variants	Comment	Organism
C136S	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
C285S	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
C58S	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
C85S	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
E14C/S29C/C85S/C73S	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
Q227C	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
Q272C	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
S190C	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida
S48C	site-directed mutagenesis, putidaredoxin binding compared to wild-type	Pseudomonas putida

Inhibitors

Inhibitors	Comment	Organism	Structure
Metyrapone	enzyme P450cam bound to metyrapone is constrained in the closed conformation	Pseudomonas putida

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	interaction thermodynamics between Pdx and various states of P450cam constrained in different conformations, overview	Pseudomonas putida

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	enzyme-bound	Pseudomonas putida

Natural Substrates/ Products (Substrates)

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

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	-	?
additional information	enzyme 450cam binds camphor and converts from the closed to open conformation upon binding putidaredoxin, the binding thermodynamics of Pdx differ when the conformation of P450cam is held in different states, thermodynamic analysis, overview	Pseudomonas putida	?	-	?

Synonyms

Synonyms	Comment	Organism
camphor monooxygenase	-	Pseudomonas putida
CYP101A1	-	Pseudomonas putida
P450cam	-	Pseudomonas putida

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
20	-	assay at	Pseudomonas putida

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Pseudomonas putida

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome P450	-	Pseudomonas putida
putidaredoxin	Pdx, the enzyme is highly specific for its reductase, with an absolute requirement for the native putidaredoxin (Pdx) to provide the second electron transfer, binding kinetics and thermodynamics with wild-type and mutant enzymes, overview. Upon binding ferric P450cam, Pdx is now known to trigger a conformational change in the enzyme, which may provide the trigger to coordinate enzyme turnover and protect the enzyme from oxidative damage	Pseudomonas putida

General Information

General Information	Comment	Organism
evolution	cytochrome P450cam (CYP101) from Pseudomonas putida is the model enzyme for the P450 superfamily	Pseudomonas putida
additional information	double electron-electron resonance measurements of intermolecular distances in the Pdx/P450cam complex show that the geometry of the complex is nearly identical for the open and closed states of P450cam	Pseudomonas putida
physiological function	cytochrome P450cam carries out the conversion of camphor to 5-exohydroxycamphor under conditions in which the bacterium uses camphor as the primary carbon source for growth	Pseudomonas putida

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Release 2023.1 (January 2023)