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show all sequences of 1.14.14.133

Crystal structure of cindoxin, the P450cin redox partner

Madrona, Y.; Hollingsworth, S.; Tripathi, S.; Fields, J.; Rwigema, J.; Tobias, D.; Poulos, T.; Biochemistry 53, 1435-1446 (2014)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
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
Engineering
Amino acid exchange
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2
Citrobacter braakii
-
2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Citrobacter braakii
Q8VQF6
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2
-
744316
Citrobacter braakii
2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
30
assay at
Citrobacter braakii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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
Commentary
Organism
7.5
-
assay at
Citrobacter braakii
Cofactor
Cofactor
Commentary
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
Activating Compound (protein specific)
Activating Compound
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
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
Engineering (protein specific)
Amino acid exchange
Commentary
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] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
stopped-flow oxyP450cin formation and P450cin-Cdx electron transfer analysis
Citrobacter braakii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2
Citrobacter braakii
-
2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,8-cineole + [reduced NADPH-hemoprotein reductase] + O2
-
744316
Citrobacter braakii
2-endo-hydroxy-1,8-cineole + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
30
assay at
Citrobacter braakii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
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 (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Citrobacter braakii
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 1.14.14.133
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
746360
Belsare
Directed evolution of P450cin ...
Citrobacter braakii
Protein Eng. Des. Sel.
30
119-127
2017
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2
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744316
Madrona
Crystal structure of cindoxin ...
Citrobacter braakii
Biochemistry
53
1435-1446
2014
1
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1
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1
1
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717156
Slessor
Oxygen activation by P450(cin) ...
Citrobacter braakii
Arch. Biochem. Biophys.
507
154-162
2011
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3
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1
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4
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717493
Hawkes
Cloning, expression and purifi ...
Citrobacter braakii
ChemBioChem
11
1107-1114
2010
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1
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1
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717775
Meharenna
The critical role of substrate ...
Citrobacter braakii
J. Biol. Chem.
283
10804-10812
2008
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1
1
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2
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717774
Kimmich
Electron transfer between cyto ...
Citrobacter braakii
J. Biol. Chem.
282
27006-27011
2007
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717238
Meharenna
Crystal structure of P450cin i ...
Citrobacter braakii
Biochemistry
43
9487-9494
2004
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1
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1
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717765
Hawkes
Cytochrome P450(cin) (CYP176A) ...
Citrobacter braakii
J. Biol. Chem.
277
27725-27732
2002
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1
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1
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