Literature summary for 1.14.14.133 extracted from

Madrona, Y.; Hollingsworth, S.; Tripathi, S.; Fields, J.; Rwigema, J.; Tobias, D.; Poulos, T.
Crystal structure of cindoxin, the P450cin redox partner (2014), Biochemistry, 53, 1435-1446 .

Search for more literature for 1.14.14.133

Activating Compound

Activating Compound	Comment	Organism	Structure
cindoxin	Cdx, UniProt ID Q8VQF4, the FMN-containing redox partner to P450cin. Brownian dynamics-molecular dynamics docking method is used to produce a model of Cdx with its redox partner, enzyme P450cin, overview. Potential importance of Cdx Tyr96 in bridging the FMN and heme cofactors as well P450cin Arg102 and Arg346. Arg346 plays an important role in electron transfer. Arg102 also interacts with a P450cin heme propionate. Redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex. Crystal structure determination of wild-type and mutant cindoxins	Citrobacter braakii

Protein Variants

Protein Variants	Comment	Organism
R102A	site-directed mutagenesis, the mutant is unable to bind the redox partner cindoxin and shows only 5% of wild-type enzyme NADPH turnover	Citrobacter braakii
R346A	site-directed mutagenesis, the mutant is unable to bind the redox partner cindoxin and shows only 10% of wild-type enzyme NADPH turnover	Citrobacter braakii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	stopped-flow oxyP450cin formation and P450cin-Cdx electron transfer analysis	Citrobacter braakii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2	Citrobacter braakii	-	2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Citrobacter braakii	Q8VQF6	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2	-	Citrobacter braakii	2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O	-	?

Synonyms

Synonyms	Comment	Organism
CinA	-	Citrobacter braakii
P450cin	-	Citrobacter braakii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
22	30	assay at	Citrobacter braakii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
44	-	[reduced NADPH-hemoprotein reductase]	pH 7.5, 22°C, P450cin mutant R346A	Citrobacter braakii
82.4	-	[reduced NADPH-hemoprotein reductase]	pH 7.5, 22°C, P450cin mutant R102A	Citrobacter braakii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Citrobacter braakii

Cofactor

Cofactor	Comment	Organism	Structure
cytochrome P-450	-	Citrobacter braakii
NADPH-hemoprotein reductase	A flavoprotein containing both FMN and FAD. This enzyme catalyses the transfer of electrons from NADPH, an obligatory two-electron donor, to microsomal P-450 monooxygenases, EC 1.14.14._	Citrobacter braakii

General Information

General Information	Comment	Organism
additional information	redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex	Citrobacter braakii

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Release 2023.1 (January 2023)