Any feedback?
Literature summary for 1.2.1.90 extracted from
- 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.
Activating Compound
| Activating Compound | Comment | 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)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermoproteus tenax |
Inhibitors
| Inhibitors | Comment | 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 | Comment | 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 | Comment | Organism | Structure |
|---|---|---|---|
| additional information | Mg2+ does not affect the enzymatic properties | Thermoproteus tenax |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 55000 | - |
x * 55000, calculated from sequence | Thermoproteus tenax |
| 220000 | - |
- |
Thermoproteus tenax |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoproteus tenax | O57693 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Thermoproteus tenax |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + NAD+ + H2O | - |
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 | Thermoproteus tenax | 3-phospho-D-glycerate + NADH + 2 H+ | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 55000, calculated from sequence | Thermoproteus tenax |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase | - |
Thermoproteus tenax |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | - |
assay at | Thermoproteus tenax |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | 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 | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Thermoproteus tenax |
Cofactor
| Cofactor | Comment | 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 | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.13 | - |
L-Glyceraldehyde 3-phosphate | pH 7.0, 70°C | Thermoproteus tenax | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
