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Literature summary extracted from
- Cloning and characterization of two novel chloroplastic glycerol-3-phosphate dehydrogenases from Dunaliella viridis (2009), Plant Mol. Biol., 71, 193-205.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.8 | additional information | the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of GPDH1 transcript reaches a maximum in 2 M NaCl, which is about 2fold more than that in 0.5 M NaCl | Dunaliella viridis | |
| 1.1.1.8 | additional information | the GPDH genes exhibit transient transcriptional induction of gene expression upon hypersalinity shock followed by a negative feedback of gene expression, the level of isozyme GPDH2 transcript reaches a maximum in 1 M NaCl and although the GPDH2 transcript level almost remains constant in salinities ranging from 3 to 5 M NaCl | Dunaliella viridis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.8 | expressed in Escherichia coli BL21(DE3) pLysS cells | Dunaliella viridis |
| 1.1.1.8 | expressed in Escherichia coli BL21(DE3) pLysScells | Dunaliella viridis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.8 | additional information | GPDH1 transcript level decreases progressively with NaCl concentrations above 3-5 M, the expression level of GPDH1 in 5 M NaCl is only approximately a quarter of that in 2 M NaCl; the GPDH2 transcript level decreases to less than half the level in 1 M NaCl | Dunaliella viridis | |
| 1.1.1.8 | NaCl | isozyme GPDH1 is severely inhibited by the addition of 100-200 mM NaCl; isozyme GPDH2 is severely inhibited by the addition of 100-200 mM NaCl | Dunaliella viridis |  |
| 1.1.1.8 | phosphate | phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH1; phosphate at 5-10 mM severely inhibits the enzymatic activity of isozyme GPDH2 | Dunaliella viridis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.8 | 0.0589 | - |
NADPH | isozyme GPDH1 | Dunaliella viridis | |
| 1.1.1.8 | 0.0589 | - |
NADH | recombinant isozyme GDH2 | Dunaliella viridis | |
| 1.1.1.8 | 0.0592 | - |
NADH | isozyme GPDH2 | Dunaliella viridis | |
| 1.1.1.8 | 0.0592 | - |
NADPH | recombinant isozyme GDH1 | Dunaliella viridis | |
| 1.1.1.8 | 0.0726 | - |
NADPH | isozyme GPDH2 | Dunaliella viridis | |
| 1.1.1.8 | 0.0726 | - |
NADPH | recombinant isozyme GDH2 | Dunaliella viridis | |
| 1.1.1.8 | 0.0905 | - |
NADH | isozyme GPDH1 | Dunaliella viridis | |
| 1.1.1.8 | 0.0905 | - |
NADH | recombinant isozyme GDH1 | Dunaliella viridis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.1.1.8 | chloroplast | - |
Dunaliella viridis | 9507 | - |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.8 | 76200 | - |
calculated from amino acid sequence | Dunaliella viridis |
| 1.1.1.8 | 77200 | - |
calculated from amino acid sequence | Dunaliella viridis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.8 | Dunaliella viridis | C5H3W0 | - |
- |
| 1.1.1.8 | Dunaliella viridis | C5H3W0 | isozyme GPDH1 | - |
| 1.1.1.8 | Dunaliella viridis | C5H3W1 | - |
- |
| 1.1.1.8 | Dunaliella viridis | C5H3W1 | isozyme GPDH2 | - |
| 1.1.1.8 | Dunaliella viridis SHU | C5H3W0 | isozyme GPDH1 | - |
| 1.1.1.8 | Dunaliella viridis SHU | C5H3W1 | isozyme GPDH2 | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.8 | GSTrap column chromatography | Dunaliella viridis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | - |
Dunaliella viridis | dihydroxyacetone phosphate + NADH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis | dihydroxyacetone phosphate + NADH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | - |
Dunaliella viridis SHU | dihydroxyacetone phosphate + NADH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis SHU | dihydroxyacetone phosphate + NADH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | - |
Dunaliella viridis | dihydroxyacetone phosphate + NADPH + H+ | the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH | ? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | - |
Dunaliella viridis | dihydroxyacetone phosphate + NADPH + H+ | the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH | ? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis | dihydroxyacetone phosphate + NADPH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | - |
Dunaliella viridis SHU | dihydroxyacetone phosphate + NADPH + H+ | the measured GPDH activity of isozyme GPDH1 with NADH is approximately twice of that observed with NADPH | ? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | isozymes GPDH1 can utilize both NADH and NADPH as coenzymes but exhibits significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis SHU | dihydroxyacetone phosphate + NADPH + H+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NADP+ | - |
Dunaliella viridis SHU | dihydroxyacetone phosphate + NADPH + H+ | the measured GPDH activity of isozyme GPDH2 with NADH is approximately twice of that observed with NADPH | ? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.8 | GPDH1 | isozyme | Dunaliella viridis |
| 1.1.1.8 | GPDH1 | isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains | Dunaliella viridis |
| 1.1.1.8 | GPDH2 | isozyme | Dunaliella viridis |
| 1.1.1.8 | GPDH2 | isozyme, contains an extra phosphoserine phosphatase domain at the N-terminus in addition to C-terminal GPDH domains | Dunaliella viridis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.8 | NADH | isozyme GPDH1 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme | Dunaliella viridis | |
| 1.1.1.8 | NADH | isozyme GPDH1 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis | |
| 1.1.1.8 | NADH | isozyme GPDH2 can utilize both NADH and NADPH as coenzymes and exhibits significantly higher GPDH activity when NADH is used as the coenzyme | Dunaliella viridis | |
| 1.1.1.8 | NADH | isozyme GPDH2 can utilize both NADH and NADPH as coenzymes but exhibit significantly higher activities when NADH is used as the coenzyme | Dunaliella viridis | |
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