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Literature summary for 1.2.1.12 extracted from
- Cytosolic glyceraldehyde-3-phosphate dehydrogenase is phosphorylated during seed development (2017), Front. Plant Sci., 8, 522 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Codon PlusR (DE3) RIL | Ricinus communis |
| recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Codon PlusR (DE3) RIL | Triticum aestivum |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S124A | site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, but shows highly reduced activity | Triticum aestivum |
| S205A | site-directed mutagenesis, the mutant is poorly or not phosphorylated, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type | Triticum aestivum |
| S205D | site-directed mutagenesis, the mutant enzyme (mimicking the phosphorylated form) exhibits a sstrong decrease in activity but similar affinity toward substrates compared to wild-type. The catalytic efficiency is 330 and 410fold lower with NAD+ and Ga3P, respectively | Triticum aestivum |
| S66A | site-directed mutagenesis, the mutant is phosphorylated in a similar way like the wild-type enzyme, the mutant shows similar affinity for both substrates but near half of the Vmax compared to wild-type | Triticum aestivum |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.064 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant wild-type enzyme | Triticum aestivum |  |
| 0.074 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant mutant S66A | Triticum aestivum | |
| 0.08 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant mutant S205D | Triticum aestivum | |
| 0.098 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant mutant S205A | Triticum aestivum | |
| 0.122 | - |
NAD+ | pH 8.5, 30°C, recombinant mutant S205A | Triticum aestivum | |
| 0.122 | - |
NAD+ | pH 8.5, 30°C, recombinant mutant S66A | Triticum aestivum | |
| 0.126 | - |
NAD+ | pH 8.5, 30°C, recombinant wild-type enzyme | Triticum aestivum | |
| 0.13 | - |
NAD+ | pH 8.5, 30°C, recombinant mutant S205D | Triticum aestivum | |
| 0.188 | - |
D-glyceraldehyde 3-phosphate | pH 8.5, 30°C, recombinant mutant S124A | Triticum aestivum | |
| 0.299 | - |
NAD+ | pH 8.5, 30°C, recombinant mutant S124A | Triticum aestivum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Ricinus communis | 5829 | - |
| cytosol | - |
Triticum aestivum | 5829 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Ricinus communis | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Triticum aestivum | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Ricinus communis | B9RHV9 | harvested from the field around the University Campus (Biochemistry and Biological Sciences Faculty, UNL, Santa Fe, Argentina) in 2011 and 2013 | - |
| Triticum aestivum | A0A1B1V4Q3 | cv. Baguette 11 | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | cytosolic glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in vivo during seed development. In vitro phosphorylation assays with different plant protein kinases (WPK4, SOS2, GSK3, MAPK, CKII, Tsl, and CDPK), overview | Ricinus communis |
| phosphoprotein | cytosolic glyceraldehyde-3-phosphate dehydrogenase is phosphorylated in vivo during seed development. NAD-GAPDH is phosphorylated in vitro at Ser205 by a SNF1-related protein kinase 1 (SnRK1) from wheat heterotrophic (but not from photosynthetic) tissues. The S205D mutant enzyme (mimicking the phosphorylated form) exhibits a significant decrease in activity but similar affinity toward substrates. In vitro phosphorylation assays with different plant protein kinases (WPK4, SOS2, GSK3, MAPK, CKII, Tsl, and CDPK), overview. Phosphorylation assays with wheat seed extract show that S66A and S124A NAD-GAPDH mutants are phosphorylated in a similar way like the wild-type enzyme, but the S205A mutant is recalcitrant to phosphorylation in any of the conditions assayed | Triticum aestivum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21 Codon PlusR (DE3) RIL by nickel affinity chromatography | Ricinus communis |
| recombinant His-tagged enzyme from Escherichia coli strain BL21 Codon PlusR (DE3) RIL by nickel affinity chromatography | Triticum aestivum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| leaf | - |
Ricinus communis | - |
| leaf | - |
Triticum aestivum | - |
| seed | in castor oil seed, the NAD-GAPDH activity slightly increases and total protein levels do not significantly change in the first half of seed development but both abruptly decreases in the second part of development, when triacylglycerol synthesis and storage begin | Ricinus communis | - |
| seed | NAD-GAPDH activity gradually increases along wheat seed development, but protein levels and phosphorylation status exhibit only slight changes | Triticum aestivum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Ricinus communis | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
| D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Triticum aestivum | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homotetramer | 4 * 37000, SDS-PAGE | Ricinus communis |
| homotetramer | 4 * 37000, SDS-PAGE | Triticum aestivum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GapC1 | - |
Triticum aestivum |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Ricinus communis |
| glyceraldehyde-3-phosphate dehydrogenase | - |
Triticum aestivum |
| NAD-GAPDH | - |
Ricinus communis |
| NAD-GAPDH | - |
Triticum aestivum |
| TaeNAD-GAPDH | - |
Triticum aestivum |
| TagapC | - |
Triticum aestivum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Ricinus communis |
| 30 | - |
assay at | Triticum aestivum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Ricinus communis |
| 8.5 | - |
assay at | Triticum aestivum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Ricinus communis | |
| NAD+ | - |
Triticum aestivum | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate lipids (castor oil seed). In castor oil seed, the activity slightly increased and total protein levels do not significantly change in the first half of seed development but both abruptly decreases in the second part of development, when triacylglycerol synthesis and storage begin | Ricinus communis |
| physiological function | cytosolic glyceraldehyde-3-phosphate dehydrogenase (NAD-GAPDH) is involved in a critical energetic step of glycolysis and also has many important functions besides its enzymatic activity. NAD-GAPDH enzyme catalyzes the phosphorylating-coupled oxidation of glyceraldehyde 3-phosphate. Its catalytic role in glycolysis is based on a highly reactive catalytic cysteine that is often target of oxidative modifications that blocks its enzymatic activity and in turns trigger other moonlighting non-glycolytic roles. NAD-GAPDH is phosphorylated in vivo, the enzyme depicts different activity, abundance and phosphorylation profiles during development of seeds that mainly accumulate starch (wheat). NAD-GAPDH activity gradually increases along wheat seed development, but protein levels and phosphorylation status exhibit only slight changes | Triticum aestivum |
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