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show all sequences of 1.1.1.311

Crystal structure and enzyme kinetics of the (S)-specific 1-phenylethanol dehydrogenase of the denitrifying bacterium strain EbN1

Hoeffken, H.W.; Duong, M.; Friedrich, T.; Breuer, M.; Hauer, B.; Reinhardt, R.; Rabus, R.; Heider, J.; Biochemistry 45, 82-93 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpressed in Escherichia coli
Azoarcus sp.
Crystallization (Commentary)
Crystallization
Organism
sitting drop method in a buffer containing 12-18% PEG 8000, 0.05 M potassium phosphate, pH 7.5 and 3% 2-methyl-2,4-pentanediol. The structure of the apo-form of the enzyme is solved with a resolution at 2.1 A. The enzyme soaked with NAD+ and the inhibitor (R)-1-phenylethanol forms a different crystal form containing two subunits in the asymmetric unit
Azoarcus sp.
Inhibitors
Inhibitors
Commentary
Organism
Structure
(R)-1-phenylethanol
0.05 mM, 50% inhibition of acetophenone reduction activity
Azoarcus sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
4 * 27000
Azoarcus sp.
93000
-
gel filtration
Azoarcus sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azoarcus sp.
Q5P5I4
-
-
Azoarcus sp. EbN1
Q5P5I4
-
-
Purification (Commentary)
Commentary
Organism
-
Azoarcus sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-phenylethanol + NAD+
-
685078
Azoarcus sp.
acetophenone + NADH + H+
-
-
-
r
(S)-1-phenylethanol + NAD+
-
685078
Azoarcus sp. EbN1
acetophenone + NADH + H+
-
-
-
r
Subunits
Subunits
Commentary
Organism
tetramer
4 * 27000
Azoarcus sp.
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Azoarcus sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Azoarcus sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpressed in Escherichia coli
Azoarcus sp.
Crystallization (Commentary) (protein specific)
Crystallization
Organism
sitting drop method in a buffer containing 12-18% PEG 8000, 0.05 M potassium phosphate, pH 7.5 and 3% 2-methyl-2,4-pentanediol. The structure of the apo-form of the enzyme is solved with a resolution at 2.1 A. The enzyme soaked with NAD+ and the inhibitor (R)-1-phenylethanol forms a different crystal form containing two subunits in the asymmetric unit
Azoarcus sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
(R)-1-phenylethanol
0.05 mM, 50% inhibition of acetophenone reduction activity
Azoarcus sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
4 * 27000
Azoarcus sp.
93000
-
gel filtration
Azoarcus sp.
Purification (Commentary) (protein specific)
Commentary
Organism
-
Azoarcus sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-phenylethanol + NAD+
-
685078
Azoarcus sp.
acetophenone + NADH + H+
-
-
-
r
(S)-1-phenylethanol + NAD+
-
685078
Azoarcus sp. EbN1
acetophenone + NADH + H+
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 27000
Azoarcus sp.
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
25
-
assay at
Azoarcus sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Azoarcus sp.
Other publictions for EC 1.1.1.311
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)
739947
Dudzik
Asymmetric reduction of ketone ...
Aromatoleum aromaticum, Aromatoleum aromaticum EbN1
Appl. Microbiol. Biotechnol.
99
5055-5069
2015
-
1
1
1
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685078
Hoeffken
Crystal structure and enzyme k ...
Azoarcus sp., Azoarcus sp. EbN1
Biochemistry
45
82-93
2006
-
-
1
1
-
-
1
-
-
-
2
-
-
4
-
-
1
-
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
1
-
-
-
-
2
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
707292
Kniemeyer
(S)-1-Phenylethanol dehydrogen ...
Azoarcus sp., Azoarcus sp. EbN1
Arch. Microbiol.
176
129-135
2001
-
-
-
-
-
-
2
4
-
-
2
2
-
11
-
-
1
-
-
1
1
-
6
1
-
-
-
4
2
-
-
2
-
1
-
-
-
-
2
-
-
-
-
2
-
4
-
-
2
2
-
-
-
1
-
1
1
-
6
1
-
-
-
4
2
-
-
1
-
-
-
-
-
-