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Literature summary for 1.2.1.12 extracted from
- Purification and properties of glyceraldehyde-3-phosphate dehydrogenase from the skeletal muscle of the hibernating ground squirrel, Ictidomys tridecemlineatus (2014), PeerJ, 2, e634 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. Action of commercial alkaline phosphatase causes a 50% increase in euthermic GAPDH activity, activities of protein kinase C, AMP-dependent protein kinase, or calcium-calmodulin protein kinase lead to about 80% decreases in euthermic GAPDH activity | Ictidomys tridecemlineatus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetic analysis and thermodynamics of purified euthermic and torpid enzyme | Ictidomys tridecemlineatus | |
| 0.22 | - |
3-phospho-D-glyceroyl phosphate | pH 8.0, 5°C, euthermic | Ictidomys tridecemlineatus |  |
| 0.24 | - |
3-phospho-D-glyceroyl phosphate | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
| 0.24 | - |
3-phospho-D-glyceroyl phosphate | pH 8.0, 5°C, euthermic | Ictidomys tridecemlineatus | |
| 0.28 | - |
3-phospho-D-glyceroyl phosphate | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
| 0.45 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 5°C, euthermic | Ictidomys tridecemlineatus | |
| 0.47 | - |
NAD+ | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
| 0.5 | - |
NAD+ | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
| 0.52 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 5°C, euthermic | Ictidomys tridecemlineatus | |
| 1.3 | - |
NAD+ | pH 8.0, 5°C, euthermic | Ictidomys tridecemlineatus | |
| 1.4 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
| 1.5 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 36°C, long torpor | Ictidomys tridecemlineatus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Ictidomys tridecemlineatus | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ictidomys tridecemlineatus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| acetylation | - |
Ictidomys tridecemlineatus |
| alkylation | methylation on residues Lys213 and Asp242, site specific alterations in methylation sites suggests that the stable changes observed in kinetic and structural GAPDH properties may be due to posttranslational modification of this enzyme during torpor | Ictidomys tridecemlineatus |
| phosphoprotein | posttranslational phosphorylation on tyrosine residues, global reduction in GAPDH tyrosine phosphorylation during torpor that the stable changes observed in kinetic and structural GAPDH properties may be due to posttranslational modification of this enzyme during torpor. GAPDH regulation by reversible phosphorylation, action of commercial alkaline phosphatase causes a 50% increase in euthermic GAPDH activity, activities of protein kinase C, AMP-dependent protein kinase, or calcium-calmodulin protein kinase lead to about 80% decreases in euthermic GAPDH activity | Ictidomys tridecemlineatus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme 430fold by affinity and hydrophobic interaction chromatography | Ictidomys tridecemlineatus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | - |
Ictidomys tridecemlineatus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 146 | - |
purified enzyme, pH 8.0, 25°C | Ictidomys tridecemlineatus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
Ictidomys tridecemlineatus | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
r | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Ictidomys tridecemlineatus | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 37000, about | Ictidomys tridecemlineatus |
| More | peptide mapping, mass spectrometry, overview | Ictidomys tridecemlineatus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GAPDH | - |
Ictidomys tridecemlineatus |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Ictidomys tridecemlineatus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 5 | 36 | assay at | Ictidomys tridecemlineatus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 34 | 55 | long topor GAPDH is significantly less susceptible to thermal denaturation as compared to euthermic GAPDH, with 45°C or 55°C being required to cause a significant decrease in long topor GAPDH enzyme activity as compared to 35-45°C for euthermic GAPDH. Long topor GAPDH displays a significantly higher thermal melting point of 56.1°C as compared to the euthermic GAPDH Tm of 54.7°C | Ictidomys tridecemlineatus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
both reaction directions | Ictidomys tridecemlineatus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Ictidomys tridecemlineatus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | diverse functions of GAPDH, including roles in membrane trafficking, apoptosis, and autophagy in addition to GAPDH's canonical role within the glycolytic and gluconeogenic pathways. In this capacity it converts D-glyceraldehyde-3-phosphate and NAD+ to 1,3-bisphosphoglycerate and NADH in the glycolytic pathway, or the reverse reaction in the gluconeogenic pathway. GAPDH plays a central role in carbohydrate metabolismin ground squirrels, which typically shift to non-carbohydrate fuels during winter hibernation, stable suppression of GAPDH (possibly by some reversible posttranslational modification) during ground squirrel torpor, which likely contributes to the overall reduction in carbohydrate metabolism when these animals switch to lipid fuels during dormancy. GAPDH regulation by reversible phosphorylation | Ictidomys tridecemlineatus |
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