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show all sequences of 1.1.1.11

Cloning, purification and characterization of an NAD-dependent D-arabitol dehydrogenase from acetic acid bacterium, Acetobacter suboxydans

Cheng, H.; Li, Z.; Jiang, N.; Deng, Z.; Protein J. 28, 263-272 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-arabitol
inducer
Gluconobacter oxydans
Application
Application
Commentary
Organism
industry
promising method for the production of xylitol from the cheap material glucose if the aArDH gene can be introduced into yeast strains that can convert glucose to D-arabitol
Gluconobacter oxydans
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli; expression vector containing the ORF of aArDH under the control of T7 promoter, pET21aArDH, transformed into Escherichia coli strain BL21(DE3)
Gluconobacter oxydans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
10 mM, complete inhibition. Activity can partly be restored by addition of EDTA
Gluconobacter oxydans
CuSO4
inactivates aArDH activity, which is restored by 80% by addition of 100 mM EDTA at pH 8.0
Gluconobacter oxydans
Zn2+
up to 200 mM, slight inhibition
Gluconobacter oxydans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.5
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
4.5
-
D-arabitol
-
Gluconobacter oxydans
18.5
-
xylitol
-
Gluconobacter oxydans
78.5
-
D-mannitol
; pH 8.5, 25°C
Gluconobacter oxydans
127.3
-
D-sorbitol
; pH 8.5, 25°C
Gluconobacter oxydans
133.6
-
glycerol
; pH 8.5, 25°C
Gluconobacter oxydans
177.2
-
xylitol
pH 8.5, 25°C
Gluconobacter oxydans
242.8
-
ribitol
; pH 8.5, 25°C
Gluconobacter oxydans
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ba2+
up to 200 mM, 2fold increase in activity
Gluconobacter oxydans
Ca2+
up to 200 mM, 2fold increase in activity
Gluconobacter oxydans
additional information
not stimulatory: Mn2+, Ni2+, Mg2+
Gluconobacter oxydans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
4 * 28500, calculated, 4 * 28000, SDS-PAGE
Gluconobacter oxydans
28500
-
4 * 28500, calculated, 4 * 28000, SDS-PAGE; native aArDH, 2 * 28500, SDS-PAGE; recombinant aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
140000
-
gel filtration
Gluconobacter oxydans
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gluconobacter oxydans
-
-
-
Gluconobacter oxydans
Q308C1
-
-
Purification (Commentary)
Commentary
Organism
; recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
Gluconobacter oxydans
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.14
-
crude extract
Gluconobacter oxydans
0.55
-
recombinant aArDH with meso-erythritol as substrate
Gluconobacter oxydans
0.87
-
recombinant aArDH with ethanol as substrate
Gluconobacter oxydans
1.5
-
recombinant aArDH with ribitol as substrate
Gluconobacter oxydans
2.1
-
recombinant aArDH with glycerol as substrate
Gluconobacter oxydans
2.5
-
recombinant aArDH with D-fructose as substrate
Gluconobacter oxydans
2.8
-
recombinant aArDH with D-sorbitol as substrate
Gluconobacter oxydans
4.2
-
recombinant aArDH with D-mannitol as substrate
Gluconobacter oxydans
12.6
-
recombinant aArDH with xylitol as substrate
Gluconobacter oxydans
16.4
-
recombinant aArDH with D-xylulose as substrate
Gluconobacter oxydans
16.66
-
119fold purified enzyme
Gluconobacter oxydans
68.5
-
pH 8.5, 25°C; recombinant aArDH with 100 mM D-arabitol as substrate
Gluconobacter oxydans
Storage Stability
Storage Stability
Organism
4°C, 100 mM Tris/HCl buffer, 2 mM 2-mercaptoethanol, 50 days
Gluconobacter oxydans
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol for 50 days, 50% loss of activity. Addition of 2-mercaptoethanol is required
Gluconobacter oxydans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinitol + NAD+
-
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
r
D-arabitol + NAD+
is the optimal substrate for aArDH
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
r
D-fructose + NADH + H+
-
701082
Gluconobacter oxydans
D-mannitol + NAD+
-
-
-
?
D-mannitol + NAD+
-
701082
Gluconobacter oxydans
D-fructose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
-
701082
Gluconobacter oxydans
L-sorbose + NADH + H+
-
-
-
?
D-xylulose + NADH + H+
-
701082
Gluconobacter oxydans
D-arabitol + NAD+
-
-
-
r
ethanol + NAD+
-
701082
Gluconobacter oxydans
acetaldehyde + NADH + H+
-
-
-
?
glycerol + NAD+
-
701082
Gluconobacter oxydans
dihydroxyacetone + NADH + H+
-
-
-
?
meso-erythritol + NAD+
-
701082
Gluconobacter oxydans
? + NADH + H+
-
-
-
?
additional information
both purified native and recombinant aArDH do not accept L-arabitol as substrate
701082
Gluconobacter oxydans
?
-
-
-
-
additional information
no substrate: L-arabinitol
701082
Gluconobacter oxydans
?
-
-
-
-
ribitol + NAD+
-
701082
Gluconobacter oxydans
D-ribulose + NADH + H+
-
-
-
?
xylitol + NAD+
-
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterodimer
native aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
homodimer
recombinant aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
tetramer
4 * 28500, calculated, 4 * 28000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Gluconobacter oxydans
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Gluconobacter oxydans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.4
-
ribitol
; pH 8.5, 25°C
Gluconobacter oxydans
16.3
-
glycerol
; pH 8.5, 25°C
Gluconobacter oxydans
19.7
-
D-sorbitol
; pH 8.5, 25°C
Gluconobacter oxydans
35.3
-
D-mannitol
; pH 8.5, 25°C
Gluconobacter oxydans
177.2
-
xylitol
; pH 8.5, 25°C
Gluconobacter oxydans
876
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
876
-
D-arabitol
-
Gluconobacter oxydans
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
optimum for ketone reduction
Gluconobacter oxydans
8.5
-
optimum for polyol oxidation; optimum pH for oxidation is 8.5, with 0.7% and 5.6% of the maximum activity at pH 5.0 and 14, respectively. Optimal pH for reduction is 5.5, with 2 and 10% of the maximum activity at pH 4.5 and 8.0
Gluconobacter oxydans
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
8.5
12
very stable in alkaline buffer
Gluconobacter oxydans
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
aArDH prefers NAD+ to NADP+ as coenzyme; NAD+ is preferred over NADP+
Gluconobacter oxydans
NADP+
; NAD+ is preferred over NADP+
Gluconobacter oxydans
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Gluconobacter oxydans
isoelectric focusing
-
5.88
Gluconobacter oxydans
isoelectric focusing
-
5.9
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-arabitol
inducer
Gluconobacter oxydans
Application (protein specific)
Application
Commentary
Organism
industry
promising method for the production of xylitol from the cheap material glucose if the aArDH gene can be introduced into yeast strains that can convert glucose to D-arabitol
Gluconobacter oxydans
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Gluconobacter oxydans
expression vector containing the ORF of aArDH under the control of T7 promoter, pET21aArDH, transformed into Escherichia coli strain BL21(DE3)
Gluconobacter oxydans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
aArDH prefers NAD+ to NADP+ as coenzyme
Gluconobacter oxydans
NAD+
NAD+ is preferred over NADP+
Gluconobacter oxydans
NADP+
-
Gluconobacter oxydans
NADP+
NAD+ is preferred over NADP+
Gluconobacter oxydans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
10 mM, complete inhibition. Activity can partly be restored by addition of EDTA
Gluconobacter oxydans
CuSO4
inactivates aArDH activity, which is restored by 80% by addition of 100 mM EDTA at pH 8.0
Gluconobacter oxydans
Zn2+
up to 200 mM, slight inhibition
Gluconobacter oxydans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.5
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
4.5
-
D-arabitol
-
Gluconobacter oxydans
18.5
-
xylitol
-
Gluconobacter oxydans
78.5
-
D-mannitol
-
Gluconobacter oxydans
78.5
-
D-mannitol
pH 8.5, 25°C
Gluconobacter oxydans
127.3
-
D-sorbitol
-
Gluconobacter oxydans
127.3
-
D-sorbitol
pH 8.5, 25°C
Gluconobacter oxydans
133.6
-
glycerol
-
Gluconobacter oxydans
133.6
-
glycerol
pH 8.5, 25°C
Gluconobacter oxydans
177.2
-
xylitol
pH 8.5, 25°C
Gluconobacter oxydans
242.8
-
ribitol
-
Gluconobacter oxydans
242.8
-
ribitol
pH 8.5, 25°C
Gluconobacter oxydans
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ba2+
up to 200 mM, 2fold increase in activity
Gluconobacter oxydans
Ca2+
up to 200 mM, 2fold increase in activity
Gluconobacter oxydans
additional information
not stimulatory: Mn2+, Ni2+, Mg2+
Gluconobacter oxydans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28000
-
4 * 28500, calculated, 4 * 28000, SDS-PAGE
Gluconobacter oxydans
28500
-
native aArDH, 2 * 28500, SDS-PAGE; recombinant aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
28500
-
4 * 28500, calculated, 4 * 28000, SDS-PAGE
Gluconobacter oxydans
140000
-
gel filtration
Gluconobacter oxydans
Purification (Commentary) (protein specific)
Commentary
Organism
-
Gluconobacter oxydans
recombinant and native enzymes purified to homogeneity by ammonium sulfate precipitation and gel filtration, 119fold
Gluconobacter oxydans
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.14
-
crude extract
Gluconobacter oxydans
0.55
-
recombinant aArDH with meso-erythritol as substrate
Gluconobacter oxydans
0.87
-
recombinant aArDH with ethanol as substrate
Gluconobacter oxydans
1.5
-
recombinant aArDH with ribitol as substrate
Gluconobacter oxydans
2.1
-
recombinant aArDH with glycerol as substrate
Gluconobacter oxydans
2.5
-
recombinant aArDH with D-fructose as substrate
Gluconobacter oxydans
2.8
-
recombinant aArDH with D-sorbitol as substrate
Gluconobacter oxydans
4.2
-
recombinant aArDH with D-mannitol as substrate
Gluconobacter oxydans
12.6
-
recombinant aArDH with xylitol as substrate
Gluconobacter oxydans
16.4
-
recombinant aArDH with D-xylulose as substrate
Gluconobacter oxydans
16.66
-
119fold purified enzyme
Gluconobacter oxydans
68.5
-
recombinant aArDH with 100 mM D-arabitol as substrate
Gluconobacter oxydans
68.5
-
pH 8.5, 25°C
Gluconobacter oxydans
Storage Stability (protein specific)
Storage Stability
Organism
4°C, 100 mM Tris/HCl buffer, 2 mM 2-mercaptoethanol, 50 days
Gluconobacter oxydans
4°C, 100 mM Tris/HCl with 2 mM 2-mercaptoethanol for 50 days, 50% loss of activity. Addition of 2-mercaptoethanol is required
Gluconobacter oxydans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinitol + NAD+
-
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
r
D-arabitol + NAD+
is the optimal substrate for aArDH
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
r
D-fructose + NADH + H+
-
701082
Gluconobacter oxydans
D-mannitol + NAD+
-
-
-
?
D-mannitol + NAD+
-
701082
Gluconobacter oxydans
D-fructose + NADH + H+
-
-
-
?
D-sorbitol + NAD+
-
701082
Gluconobacter oxydans
L-sorbose + NADH + H+
-
-
-
?
D-xylulose + NADH + H+
-
701082
Gluconobacter oxydans
D-arabitol + NAD+
-
-
-
r
ethanol + NAD+
-
701082
Gluconobacter oxydans
acetaldehyde + NADH + H+
-
-
-
?
glycerol + NAD+
-
701082
Gluconobacter oxydans
dihydroxyacetone + NADH + H+
-
-
-
?
meso-erythritol + NAD+
-
701082
Gluconobacter oxydans
? + NADH + H+
-
-
-
?
additional information
both purified native and recombinant aArDH do not accept L-arabitol as substrate
701082
Gluconobacter oxydans
?
-
-
-
-
additional information
no substrate: L-arabinitol
701082
Gluconobacter oxydans
?
-
-
-
-
ribitol + NAD+
-
701082
Gluconobacter oxydans
D-ribulose + NADH + H+
-
-
-
?
xylitol + NAD+
-
701082
Gluconobacter oxydans
D-xylulose + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
native aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
homodimer
recombinant aArDH, 2 * 28500, SDS-PAGE
Gluconobacter oxydans
tetramer
4 * 28500, calculated, 4 * 28000, SDS-PAGE
Gluconobacter oxydans
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Gluconobacter oxydans
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
30
50
optimal temperature for oxidation is at 30°C, with 2% of the maximum activity at 50°C
Gluconobacter oxydans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
13.4
-
ribitol
-
Gluconobacter oxydans
13.4
-
ribitol
pH 8.5, 25°C
Gluconobacter oxydans
16.3
-
glycerol
-
Gluconobacter oxydans
16.3
-
glycerol
pH 8.5, 25°C
Gluconobacter oxydans
19.7
-
D-sorbitol
-
Gluconobacter oxydans
19.7
-
D-sorbitol
pH 8.5, 25°C
Gluconobacter oxydans
35.3
-
D-mannitol
-
Gluconobacter oxydans
35.3
-
D-mannitol
pH 8.5, 25°C
Gluconobacter oxydans
177.2
-
xylitol
-
Gluconobacter oxydans
177.2
-
xylitol
pH 8.5, 25°C
Gluconobacter oxydans
876
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
876
-
D-arabitol
-
Gluconobacter oxydans
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
5.5
-
optimum for ketone reduction
Gluconobacter oxydans
8.5
-
optimum pH for oxidation is 8.5, with 0.7% and 5.6% of the maximum activity at pH 5.0 and 14, respectively. Optimal pH for reduction is 5.5, with 2 and 10% of the maximum activity at pH 4.5 and 8.0
Gluconobacter oxydans
8.5
-
optimum for polyol oxidation
Gluconobacter oxydans
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
8.5
12
very stable in alkaline buffer
Gluconobacter oxydans
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Gluconobacter oxydans
isoelectric focusing
-
5.88
Gluconobacter oxydans
isoelectric focusing
-
5.9
Expression
Organism
Commentary
Expression
Gluconobacter oxydans
induced by D-arabinitol
up
Expression (protein specific)
Organism
Commentary
Expression
Gluconobacter oxydans
induced by D-arabinitol
up
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.06
-
ribitol
pH 8.5, 25°C
Gluconobacter oxydans
0.12
-
glycerol
pH 8.5, 25°C
Gluconobacter oxydans
0.15
-
D-sorbitol
pH 8.5, 25°C
Gluconobacter oxydans
0.45
-
D-mannitol
pH 8.5, 25°C
Gluconobacter oxydans
9.58
-
xylitol
pH 8.5, 25°C
Gluconobacter oxydans
194.7
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.06
-
ribitol
pH 8.5, 25°C
Gluconobacter oxydans
0.12
-
glycerol
pH 8.5, 25°C
Gluconobacter oxydans
0.15
-
D-sorbitol
pH 8.5, 25°C
Gluconobacter oxydans
0.45
-
D-mannitol
pH 8.5, 25°C
Gluconobacter oxydans
9.58
-
xylitol
pH 8.5, 25°C
Gluconobacter oxydans
194.7
-
D-arabinitol
pH 8.5, 25°C
Gluconobacter oxydans
Other publictions for EC 1.1.1.11
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)
701082
Cheng
Cloning, purification and char ...
Gluconobacter oxydans
Protein J.
28
263-272
2009
1
1
1
-
-
-
3
8
-
3
3
-
-
4
-
-
1
-
-
-
12
2
18
3
1
1
-
7
2
-
1
2
-
2
-
1
1
2
4
-
-
-
-
3
-
12
-
3
4
-
-
-
-
2
-
-
13
2
18
3
1
1
-
12
3
-
1
2
1
-
-
1
6
6
670549
LaFayette
Arabitol dehydrogenase as a se ...
Escherichia coli, Escherichia coli C
Plant Cell Rep.
24
596-602
2005
-
1
1
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285753
Murray
Isolation, characterization an ...
Candida tropicalis
Gene
155
123-128
1995
-
-
1
-
-
-
-
-
-
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2
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