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Literature summary extracted from

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

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.2.1.90 ADP
-
 Thermoproteus tenax
1.2.1.90 AMP
-
 Thermoproteus tenax
1.2.1.90 D-Fructose 1-phosphate
-
 Thermoproteus tenax
1.2.1.90 D-fructose 6-phosphate
-
 Thermoproteus tenax
1.2.1.90 D-glucose 1-phosphate
-
 Thermoproteus tenax
1.2.1.90 D-glucose 6-phosphate
-
 Thermoproteus tenax
1.2.1.90 D-ribose 5-phosphate
-
 Thermoproteus tenax

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.2.1.90 expression in Escherichia coli Thermoproteus tenax

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.90 ATP
-
 Thermoproteus tenax
1.2.1.90 L-Glyceraldehyde 3-phosphate strong competitive inhibitor with respect to D-glyceraldehyde 3-phosphate Thermoproteus tenax
1.2.1.90 NADH
-
 Thermoproteus tenax
1.2.1.90 NADP+
-
 Thermoproteus tenax
1.2.1.90 NADPH
-
 Thermoproteus tenax

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.2.1.90 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
1.2.1.90 3.1
-
 NAD+ pH 7.0, 70°C, recombinant enzyme Thermoproteus tenax
1.2.1.90 3.3
-
 NAD+ pH 7.0, 70°C, enzyme isolated from Thermoproteus tenax Thermoproteus tenax

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.2.1.90 additional information Mg2+ does not affect the enzymatic properties Thermoproteus tenax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.90 55000
-
 x * 55000, calculated from sequence Thermoproteus tenax
1.2.1.90 220000
-
-
 Thermoproteus tenax

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.90 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

EC Number Organism UniProt Comment Textmining
1.2.1.90 Thermoproteus tenax O57693
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.1.90
-
 Thermoproteus tenax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.90 D-glyceraldehyde 3-phosphate + NAD+ + H2O
-
 Thermoproteus tenax 3-phospho-D-glycerate + NADH + 2 H+
-
 ir
1.2.1.90 D-glyceraldehyde 3-phosphate + NAD+ + H2O part of the modified Emden-Meyerhof-Parnas pathway in Thermoproteus tenax Thermoproteus tenax 3-phospho-D-glycerate + NADH + 2 H+
-
 ir

Subunits

EC Number Subunits Comment Organism
1.2.1.90 ? x * 55000, calculated from sequence Thermoproteus tenax

Synonyms

EC Number Synonyms Comment Organism
1.2.1.90 NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase
-
 Thermoproteus tenax

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.90 70
-
 assay at Thermoproteus tenax

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.90 100
-
 100 min, recombinant enzyme loses 90% of its activity, the enzyme isolated from Thermoproteus tenax loses 70% of its activity Thermoproteus tenax

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.90 7
-
 assay at Thermoproteus tenax

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.90 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]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.90 0.13
-
 L-Glyceraldehyde 3-phosphate pH 7.0, 70°C Thermoproteus tenax