BRENDA - Enzyme Database show
show all sequences of 1.1.1.60

Tartronate semialdehyde reductase defines a novel rate-limiting step in assimilation and bioconversion of glycerol in Ustilago maydis

Liu, Y.; Koh, C.; Sun, L.; Ji, L.; PLoS ONE 6, e16438 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Ustilago maydis
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
severe inhibition
Ustilago maydis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00019
-
2-hydroxy-3-oxopropanoate
pH 8.5, 40C
Ustilago maydis
0.0003
-
NADP+
pH 8.5, 40C
Ustilago maydis
0.0143
-
NADH
pH 8.5, 40C
Ustilago maydis
0.0177
-
D-glycerate
pH 8.5, 40C
Ustilago maydis
0.123
-
L-Glycerate
pH 8.5, 40C
Ustilago maydis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
41000
-
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
85000
-
gel filtration
Ustilago maydis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ustilago maydis
Q4PBC1
putative
-
Storage Stability
Storage Stability
Organism
4C, phosphate buffer, pH 7.0, improved solubility
Ustilago maydis
4C, Tris-HCl, pH 8.0, highly unstable, precipitates during storage
Ustilago maydis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxy-3-oxopropanoate + NADH + H+
-
726270
Ustilago maydis
D-glycerate + NAD+
-
-
-
?
D-glycerate + NADP+
enzyme shows strong specificity and enantioselectivity for D-glycerate
726270
Ustilago maydis
2-hydroxy-3-oxopropanoate + NADPH + H+
-
-
-
?
L-glycerate + NADP+
enzyme shows strong specificity and enantioselectivity for D-glycerate
726270
Ustilago maydis
2-hydroxy-3-oxopropanoate + NADPH + H+
-
-
-
?
additional information
poor activity towards 6-phosphogluconic acid, beta-hydroxybutyric acid and D-threonine
726270
Ustilago maydis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
-
Ustilago maydis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Ustilago maydis
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6.5
-
rapidly precipitates below
Ustilago maydis
7
-
phosphate buffer, pH 7.0, improved solubility
Ustilago maydis
8
-
Tris-HCl, highly unstable, precipitates during storage
Ustilago maydis
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
about 75% of the activity with NADP+
Ustilago maydis
NADP+
preferred over NAD+
Ustilago maydis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Ustilago maydis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
about 75% of the activity with NADP+
Ustilago maydis
NADP+
preferred over NAD+
Ustilago maydis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
severe inhibition
Ustilago maydis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.00019
-
2-hydroxy-3-oxopropanoate
pH 8.5, 40C
Ustilago maydis
0.0003
-
NADP+
pH 8.5, 40C
Ustilago maydis
0.0143
-
NADH
pH 8.5, 40C
Ustilago maydis
0.0177
-
D-glycerate
pH 8.5, 40C
Ustilago maydis
0.123
-
L-Glycerate
pH 8.5, 40C
Ustilago maydis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
41000
-
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
85000
-
gel filtration
Ustilago maydis
Storage Stability (protein specific)
Storage Stability
Organism
4C, phosphate buffer, pH 7.0, improved solubility
Ustilago maydis
4C, Tris-HCl, pH 8.0, highly unstable, precipitates during storage
Ustilago maydis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-hydroxy-3-oxopropanoate + NADH + H+
-
726270
Ustilago maydis
D-glycerate + NAD+
-
-
-
?
D-glycerate + NADP+
enzyme shows strong specificity and enantioselectivity for D-glycerate
726270
Ustilago maydis
2-hydroxy-3-oxopropanoate + NADPH + H+
-
-
-
?
L-glycerate + NADP+
enzyme shows strong specificity and enantioselectivity for D-glycerate
726270
Ustilago maydis
2-hydroxy-3-oxopropanoate + NADPH + H+
-
-
-
?
additional information
poor activity towards 6-phosphogluconic acid, beta-hydroxybutyric acid and D-threonine
726270
Ustilago maydis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 40000, SDS-PAGE, 2 * 41000, calculated, recombinant protein
Ustilago maydis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
40
-
-
Ustilago maydis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Ustilago maydis
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6.5
-
rapidly precipitates below
Ustilago maydis
7
-
phosphate buffer, pH 7.0, improved solubility
Ustilago maydis
8
-
Tris-HCl, highly unstable, precipitates during storage
Ustilago maydis
General Information
General Information
Commentary
Organism
physiological function
over-expression of the gene results in improved glycerol assimilation. Glycolipid accumulation is reduced by 45.2% in the knockout mutant whereas over-expression of the gene increases it by 40.4%
Ustilago maydis
General Information (protein specific)
General Information
Commentary
Organism
physiological function
over-expression of the gene results in improved glycerol assimilation. Glycolipid accumulation is reduced by 45.2% in the knockout mutant whereas over-expression of the gene increases it by 40.4%
Ustilago maydis
Other publictions for EC 1.1.1.60
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)
737745
Hoover
Identification of catalyticall ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
Biochim. Biophys. Acta
1834
2663-2671
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
726270
Liu
Tartronate semialdehyde reduct ...
Ustilago maydis
PLoS ONE
6
e16438
2011
-
-
1
-
-
-
1
5
-
-
3
-
-
4
-
-
-
-
-
-
-
2
4
1
1
-
-
-
1
-
3
2
-
-
-
-
-
1
2
-
-
-
-
1
-
5
-
-
3
-
-
-
-
-
-
-
-
2
4
1
1
-
-
-
1
-
3
-
-
1
1
-
-
-
699856
Osipiuk
X-ray crystal structure of Gar ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Struct. Funct. Genomics
10
249-253
2009
-
-
1
1
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287168
Njau
New developments in our unders ...
Escherichia coli, Haemophilus influenzae
Chem. Biol. Interact.
130-132
785-791
2001
-
-
2
-
-
-
2
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287167
Ijau
Novel beta-hydroxyacid dehydro ...
Escherichia coli, Haemophilus influenzae
J. Biol. Chem.
275
38780-38786
2000
-
-
2
-
-
-
-
5
-
-
-
-
-
4
-
-
2
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287162
Van der Drift
Glyoxylate conversion by Hypho ...
Hyphomicrobium sp.
Antonie van Leeuwenhoek
49
167-172
1983
-
-
-
-
-
-
2
1
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
4
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4589
Dijkhuizen
Metabolic regulation in Pseudo ...
Cupriavidus oxalaticus, Cupriavidus oxalaticus OX1
Arch. Microbiol.
116
77-83
1978
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287164
Kohn
Tartaric acid metabolism. 8. C ...
Pseudomonas putida
J. Biol. Chem.
243
4426-4433
1968
-
-
-
1
-
-
5
5
-
-
2
1
-
1
-
-
1
-
-
-
1
-
2
1
-
-
-
-
1
-
-
4
-
-
-
-
-
-
4
1
-
-
-
5
-
5
-
-
2
1
-
-
-
1
-
-
1
-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
287165
Kornberg
-
Tartronic semialdehyde reducta ...
Pseudomonas putida
Methods Enzymol.
9
240-247
1966
-
-
-
1
-
-
3
4
-
-
1
1
-
1
-
-
1
-
-
-
1
1
4
-
-
-
-
1
1
-
-
4
-
-
-
-
-
-
4
1
-
-
-
3
-
4
-
-
1
1
-
-
-
1
-
-
1
1
4
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
287166
Gotto
The metabolism of C2 compounds ...
Pseudomonas putida
Biochem. J.
81
273-284
1961
-
-
-
1
-
-
3
5
-
-
1
1
-
1
-
-
1
-
-
-
1
1
4
-
-
-
-
1
1
-
-
4
-
-
-
-
-
-
4
1
-
-
-
3
-
5
-
-
1
1
-
-
-
1
-
-
1
1
4
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-