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Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.133 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

EC Number Protein Variants Comment Organism
1.14.14.133 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
1.14.14.133 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]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.133 1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2 Citrobacter braakii
-
 2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.133 Citrobacter braakii Q8VQF6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.133 1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2
-
 Citrobacter braakii 2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.133 CinA
-
 Citrobacter braakii
1.14.14.133 P450cin
-
 Citrobacter braakii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.14.133 22 30 assay at Citrobacter braakii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.133 44
-
 [reduced NADPH-hemoprotein reductase] pH 7.5, 22°C, P450cin mutant R346A Citrobacter braakii
1.14.14.133 82.4
-
 [reduced NADPH-hemoprotein reductase] pH 7.5, 22°C, P450cin mutant R102A Citrobacter braakii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.14.133 7.5
-
 assay at Citrobacter braakii

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.133 cytochrome P-450
-
 Citrobacter braakii
1.14.14.133 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

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