BRENDA - Enzyme Database
show all sequences of 1.2.1.90

NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase from Thermoproteus tenax. The first identified archaeal member of the aldehyde dehydrogenase superfamily is a glycolytic enzyme with unusual regulatory properties

Brunner, N.A.; Brinkmann, H.; Siebers, B., Hensel, R.; J. Biol. Chem. 273, 6149-6156 (1998)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ADP
-
Thermoproteus tenax
AMP
-
Thermoproteus tenax
D-Fructose 1-phosphate
-
Thermoproteus tenax
D-fructose 6-phosphate
-
Thermoproteus tenax
D-glucose 1-phosphate
-
Thermoproteus tenax
D-glucose 6-phosphate
-
Thermoproteus tenax
D-ribose 5-phosphate
-
Thermoproteus tenax
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Thermoproteus tenax
Inhibitors
Inhibitors
Commentary
Organism
Structure
ATP
-
Thermoproteus tenax
L-Glyceraldehyde 3-phosphate
strong competitive inhibitor with respect to D-glyceraldehyde 3-phosphate
Thermoproteus tenax
NADH
-
Thermoproteus tenax
NADP+
-
Thermoproteus tenax
NADPH
-
Thermoproteus tenax
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
D-glyceraldehyde 3-phosphate
the saturation with D-glyceraldehyde 3-phosphate follows classical Michaelis-Menten kinetics, showing half-maximal saturation at 50 mM. A definite Km for the free aldehyde, the presumed substrate of the enzyme, cannot be given because the portion of the free aldehyde in aqueous solution could not be determined at 70 °C
Thermoproteus tenax
3.1
-
NAD+
pH 7.0, 70°C, recombinant enzyme
Thermoproteus tenax
3.3
-
NAD+
pH 7.0, 70°C, enzyme isolated from Thermoproteus tenax
Thermoproteus tenax
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
additional information
Mg2+ does not affect the enzymatic properties
Thermoproteus tenax
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 55000, calculated from sequence
Thermoproteus tenax
220000
-
-
Thermoproteus tenax
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glyceraldehyde 3-phosphate + NAD+ + H2O
Thermoproteus tenax
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
ir
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermoproteus tenax
O57693
-
-
Purification (Commentary)
Commentary
Organism
-
Thermoproteus tenax
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde 3-phosphate + NAD+ + H2O
-
727825
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
727825
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
Subunits
Subunits
Commentary
Organism
?
x * 55000, calculated from sequence
Thermoproteus tenax
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermoproteus tenax
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
100 min, recombinant enzyme loses 90% of its activity, the enzyme isolated from Thermoproteus tenax loses 70% of its activity
Thermoproteus tenax
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Thermoproteus tenax
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
NADP(H), NADH, and ATP reduce the affinity for the cosubstrate, AMP, ADP, D-glucose 1-phosphate, and D-fructose 6-phosphate increase the affinity for NAD+. Additionally, most of the effectors investigated induce cooperativity of NAD+ binding. NADP+ cannot replace NAD+
Thermoproteus tenax
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
L-Glyceraldehyde 3-phosphate
pH 7.0, 70°C
Thermoproteus tenax
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ADP
-
Thermoproteus tenax
AMP
-
Thermoproteus tenax
D-Fructose 1-phosphate
-
Thermoproteus tenax
D-fructose 6-phosphate
-
Thermoproteus tenax
D-glucose 1-phosphate
-
Thermoproteus tenax
D-glucose 6-phosphate
-
Thermoproteus tenax
D-ribose 5-phosphate
-
Thermoproteus tenax
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Thermoproteus tenax
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
NADP(H), NADH, and ATP reduce the affinity for the cosubstrate, AMP, ADP, D-glucose 1-phosphate, and D-fructose 6-phosphate increase the affinity for NAD+. Additionally, most of the effectors investigated induce cooperativity of NAD+ binding. NADP+ cannot replace NAD+
Thermoproteus tenax
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
ATP
-
Thermoproteus tenax
L-Glyceraldehyde 3-phosphate
strong competitive inhibitor with respect to D-glyceraldehyde 3-phosphate
Thermoproteus tenax
NADH
-
Thermoproteus tenax
NADP+
-
Thermoproteus tenax
NADPH
-
Thermoproteus tenax
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.13
-
L-Glyceraldehyde 3-phosphate
pH 7.0, 70°C
Thermoproteus tenax
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
D-glyceraldehyde 3-phosphate
the saturation with D-glyceraldehyde 3-phosphate follows classical Michaelis-Menten kinetics, showing half-maximal saturation at 50 mM. A definite Km for the free aldehyde, the presumed substrate of the enzyme, cannot be given because the portion of the free aldehyde in aqueous solution could not be determined at 70 °C
Thermoproteus tenax
3.1
-
NAD+
pH 7.0, 70°C, recombinant enzyme
Thermoproteus tenax
3.3
-
NAD+
pH 7.0, 70°C, enzyme isolated from Thermoproteus tenax
Thermoproteus tenax
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
additional information
Mg2+ does not affect the enzymatic properties
Thermoproteus tenax
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
55000
-
x * 55000, calculated from sequence
Thermoproteus tenax
220000
-
-
Thermoproteus tenax
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-glyceraldehyde 3-phosphate + NAD+ + H2O
Thermoproteus tenax
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
ir
Purification (Commentary) (protein specific)
Commentary
Organism
-
Thermoproteus tenax
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde 3-phosphate + NAD+ + H2O
-
727825
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
D-glyceraldehyde 3-phosphate + NAD+ + H2O
part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax
727825
Thermoproteus tenax
3-phospho-D-glycerate + NADH + 2 H+
-
-
-
ir
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 55000, calculated from sequence
Thermoproteus tenax
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
70
-
assay at
Thermoproteus tenax
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
100 min, recombinant enzyme loses 90% of its activity, the enzyme isolated from Thermoproteus tenax loses 70% of its activity
Thermoproteus tenax
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Thermoproteus tenax
Other publictions for EC 1.2.1.90
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)
728132
Lorentzen
Structural basis of allosteric ...
Thermoproteus tenax
J. Mol. Biol.
341
815-828
2004
4
-
1
1
-
-
1
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
3
-
1
-
-
-
1
-
-
2
-
-
-
4
-
1
2
1
-
-
-
1
-
-
-
-
-
1
-
-
-
1
-
-
-
-
3
-
1
-
-
-
1
-
-
-
-
1
1
-
-
-
288349
Pohl
The crystal structure of the a ...
Thermoproteus tenax
J. Biol. Chem.
277
19938-19945
2002
-
-
-
1
-
-
-
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
727454
Brunner
Role of two different glyceral ...
Thermoproteus tenax
Extremophiles
5
101-109
2001
-
-
-
-
-
-
-
3
-
-
-
1
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
727825
Brunner
NAD+-dependent glyceraldehyde- ...
Thermoproteus tenax
J. Biol. Chem.
273
6149-6156
1998
7
-
1
-
-
-
5
3
-
1
2
1
-
1
-
-
1
-
-
-
-
-
2
1
1
-
1
-
1
-
-
1
1
-
-
7
-
1
1
-
-
-
-
5
1
3
-
1
2
1
-
-
-
1
-
-
-
-
2
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-