BRENDA - Enzyme Database
show all sequences of 1.1.1.327

Biocatalytic synthesis of a diketobornane as a building block for bifunctional camphor derivatives

Hofer, M.; Strittmatter, H.; Sieber, V.; ChemCatChem 5, 3351-3357 (2013)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
synthetic route for the synthesis of bifunctional camphor derivatives. The combination of the enzymatic P450cam system with 5-exo-hydroxycamphor dehydrogenase (FdeH) allows an efficient synthesis of 2,5-diketobornane, which can be used for further derivatisation
Pseudomonas putida
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0279
-
5-exo-hydroxycamphor
pH 8.0, 45°C
Pseudomonas putida
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas putida
P09347
sequence shows one nucleotide exchange at position 336, at which replacement of a guanine by a cytosine takes place
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
5-exo-hydroxycamphor + NAD+
-
740317
Pseudomonas putida
bornane-2,5-dione + NADH + H+
-
-
-
r
bornane-2,5-dione + NADH + H+
-
740317
Pseudomonas putida
5-exo-hydroxycamphor + NAD+
-
-
-
r
additional information
no substrate: camphor
740317
Pseudomonas putida
?
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
camD
-
Pseudomonas putida
FdeH
-
Pseudomonas putida
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Pseudomonas putida
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
-
no residual activity
Pseudomonas putida
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Pseudomonas putida
Application (protein specific)
Application
Commentary
Organism
synthesis
synthetic route for the synthesis of bifunctional camphor derivatives. The combination of the enzymatic P450cam system with 5-exo-hydroxycamphor dehydrogenase (FdeH) allows an efficient synthesis of 2,5-diketobornane, which can be used for further derivatisation
Pseudomonas putida
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0279
-
5-exo-hydroxycamphor
pH 8.0, 45°C
Pseudomonas putida
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
5-exo-hydroxycamphor + NAD+
-
740317
Pseudomonas putida
bornane-2,5-dione + NADH + H+
-
-
-
r
bornane-2,5-dione + NADH + H+
-
740317
Pseudomonas putida
5-exo-hydroxycamphor + NAD+
-
-
-
r
additional information
no substrate: camphor
740317
Pseudomonas putida
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
45
-
-
Pseudomonas putida
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
60
-
no residual activity
Pseudomonas putida
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
-
Pseudomonas putida
Other publictions for EC 1.1.1.327
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
Synonyms
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)
740317
Hofer
-
Biocatalytic synthesis of a di ...
Pseudomonas putida
ChemCatChem
5
3351-3357
2013
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717268
Aramaki
Complete nucleotide sequence o ...
Pseudomonas putida, Pseudomonas putida ATCC 17453
Biochim. Biophys. Acta
1174
91-94
1993
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717740
Koga
Cloning and nucleotide sequenc ...
Pseudomonas putida
J. Biochem.
106
831-836
1989
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718333
Rheinwald
A transmissible plasmid contro ...
Pseudomonas putida
Proc. Natl. Acad. Sci. USA
70
885-889
1973
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