BRENDA - Enzyme Database show
show all sequences of 1.2.1.89

A new NAD(+)-dependent glyceraldehyde dehydrogenase obtained by rational design of l-lactaldehyde dehydrogenase from Escherichia coli

Wu, X.; Xu, L.; Yan, M.; Biosci. Biotechnol. Biochem. 80, 2306-2310 (2016)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
Escherichia coli
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
Escherichia coli
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
1.97
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
2.2
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P25553
cf. EC 1.2.1.22
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.08
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
0.13
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
1.1
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde + NAD+ + H2O
activity of mutants N286E, N286H, N286T. No substrate for wild-type
740187
Escherichia coli
D-glycerate + NADH + H+
-
-
-
?
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
55
-
1 h, 70% residual activity for mutant N286T
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
69.6
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
113.1
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
957
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
mutants N286E, N286H, N286T, but not wild-type show activtiy with NAD+
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
mutants N286E, N286H, N286T, but not wild-type show activtiy with NAD+
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
N286E
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
Escherichia coli
N286H
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde
Escherichia coli
N286T
engineering of L-lactaldehyde dehydrogenase. Contrary to wild-type, mutant is able to oxidate glyceraldehyde. Compared to L-lactaldehyde, N286T has a one-third lower Km value to glyceraldehyde.
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.14
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
1.97
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
2.2
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.08
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
0.13
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
1.1
-
mutant N286H, pH 7.0, 37°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde + NAD+ + H2O
activity of mutants N286E, N286H, N286T. No substrate for wild-type
740187
Escherichia coli
D-glycerate + NADH + H+
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
55
-
1 h, 70% residual activity for mutant N286T
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
69.6
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
113.1
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
957
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
31.64
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
99.2
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
485.8
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
31.64
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
99.2
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
485.8
-
D-glyceraldehyde
mutant N286H, pH 7.0, 37°C
Escherichia coli
Other publictions for EC 1.2.1.89
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)
740187
Wu
A new NAD(+)-dependent glycera ...
Escherichia coli
Biosci. Biotechnol. Biochem.
80
2306-2310
2016
-
-
-
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3
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3
-
-
-
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-
2
-
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-
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-
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3
-
1
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-
1
3
-
-
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1
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-
1
-
3
-
-
-
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3
-
-
-
-
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-
-
-
-
-
3
-
1
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-
1
3
-
-
-
-
-
-
-
-
3
3
739818
Iermak
-
Crystallization behaviour of g ...
Thermoplasma acidophilum
Acta Crystallogr. Sect. F
71
1475-1480
2015
-
-
1
1
1
-
-
-
-
-
-
-
-
1
-
-
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-
-
-
-
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1
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1
1
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-
-
-
-
-
726348
Steffler
Refolding of a thermostable gl ...
Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062
PLoS One
8
e70592
2013
-
1
1
-
-
-
-
1
-
-
-
-
2
6
-
-
1
-
-
-
-
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4
-
1
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1
-
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1
-
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-
1
1
1
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-
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1
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2
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1
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4
-
1
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-
-
1
-
-
-
-
-
-
-
-
-
736023
Steffler
Improvement of thermostable al ...
Thermoplasma acidophilum
Enzyme Microb. Technol.
53
307-314
2013
-
-
1
-
13
-
-
6
-
-
1
-
1
1
-
-
1
-
-
-
-
-
4
1
-
-
-
3
-
-
-
3
-
-
-
-
-
1
3
-
13
-
-
-
-
6
-
-
1
-
1
-
-
1
-
-
-
-
4
1
-
-
-
3
-
-
-
-
-
-
-
-
3
3
724216
Jung
Identification and characteriz ...
Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062
Biochem. J.
397
131-138
2006
5
-
-
-
-
-
8
2
-
-
3
2
-
8
-
-
1
-
-
-
1
-
10
2
1
1
2
-
1
1
1
1
-
-
-
5
-
-
1
-
-
-
-
8
-
2
-
-
3
2
-
-
-
1
-
-
1
-
10
2
1
1
2
-
1
1
1
-
-
1
1
-
-
-
724992
Reher
Glyceraldehyde dehydrogenases ...
Picrophilus torridus, Picrophilus torridus DSM 9790, Thermoplasma acidophilum, Thermoplasma acidophilum JCM 9062
FEBS Lett.
580
1198-1204
2006
-
-
1
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1
8
-
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6
4
-
9
-
-
2
-
-
-
1
-
18
2
4
-
4
8
4
2
-
2
-
-
-
-
-
1
2
-
-
-
-
1
-
8
-
-
6
4
-
-
-
2
-
-
1
-
18
2
4
-
4
8
4
2
-
-
-
2
2
-
8
8