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Literature summary extracted from
- Enhanced enzymatic activity of glycerol-3-phosphate dehydrogenase from the cryophilic Saccharomyces kudriavzevii (2014), PLoS ONE, 9, e87290.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.8 | additional information | the enzyme shows higher enzymatic activity in response to osmotic and cold stress | Saccharomyces kudriavzevii |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 1.1.1.8 | food industry | potential use of Saccharomyces cerevisiae-Saccharomyces kudriavzevii hybrids in the wine industry where glycerol content is an important quality parameter | Saccharomyces cerevisiae |
| 1.1.1.8 | food industry | potential use of Saccharomyces cerevisiae-Saccharomyces kudriavzevii hybrids in the wine industry where glycerol content is an important quality parameter | Saccharomyces kudriavzevii |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.8 | gene GPD1, quantitative real-time PCR expression analysis | Saccharomyces cerevisiae |
| 1.1.1.8 | gene GPD1, quantitative real-time PCR expression analysis | Saccharomyces kudriavzevii |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.8 | 0.051 | - |
NADH | at pH 7.0 and 25°C | Saccharomyces cerevisiae |  |
| 1.1.1.8 | 0.11 | - |
NADH | at pH 7.0 and 25°C | Saccharomyces kudriavzevii | |
| 1.1.1.8 | 0.54 | - |
dihydroxyacetone phosphate | at pH 7.0 and 25°C | Saccharomyces cerevisiae | |
| 1.1.1.8 | 0.61 | - |
dihydroxyacetone phosphate | at pH 7.0 and 25°C | Saccharomyces kudriavzevii | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.1.1.8 | cytoplasm | - |
Saccharomyces cerevisiae | 5737 | - |
| 1.1.1.8 | cytoplasm | - |
Saccharomyces kudriavzevii | 5737 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | Saccharomyces cerevisiae | - |
glycerone phosphate + NADH + H+ | - |
r | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | Saccharomyces kudriavzevii | - |
glycerone phosphate + NADH + H+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.8 | Saccharomyces cerevisiae | - |
- |
- |
| 1.1.1.8 | Saccharomyces cerevisiae | Q00055 | strain S288c; several strains | - |
| 1.1.1.8 | Saccharomyces cerevisiae BY4741 | - |
- |
- |
| 1.1.1.8 | Saccharomyces kudriavzevii | - |
- |
- |
| 1.1.1.8 | Saccharomyces kudriavzevii | A0A060KZ16 | several strains | - |
| 1.1.1.8 | Saccharomyces kudriavzevii IFO1802 | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.1.1.8 | additional information | glycerol production rates of different strains, overview | Saccharomyces cerevisiae | - |
| 1.1.1.8 | additional information | Saccharomyces kudriavzevii is cryophilic and grows at low temperatures (12°C). Glycerol production rates of different strains, overview | Saccharomyces kudriavzevii | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.8 | dihydroxyacetone phosphate + NADH + H+ | - |
Saccharomyces cerevisiae | sn-glycerol 3-phosphate + NAD+ | - |
? | |
| 1.1.1.8 | dihydroxyacetone phosphate + NADH + H+ | - |
Saccharomyces kudriavzevii | sn-glycerol 3-phosphate + NAD+ | - |
? | |
| 1.1.1.8 | dihydroxyacetone phosphate + NADH + H+ | - |
Saccharomyces cerevisiae BY4741 | sn-glycerol 3-phosphate + NAD+ | - |
? | |
| 1.1.1.8 | dihydroxyacetone phosphate + NADH + H+ | - |
Saccharomyces kudriavzevii IFO1802 | sn-glycerol 3-phosphate + NAD+ | - |
? | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | - |
Saccharomyces cerevisiae | glycerone phosphate + NADH + H+ | - |
r | |
| 1.1.1.8 | sn-glycerol 3-phosphate + NAD+ | - |
Saccharomyces kudriavzevii | glycerone phosphate + NADH + H+ | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.8 | GPD1 | - |
Saccharomyces cerevisiae |
| 1.1.1.8 | GPD1 | - |
Saccharomyces kudriavzevii |
| 1.1.1.8 | Gpd1p | - |
Saccharomyces cerevisiae |
| 1.1.1.8 | Gpd1p | - |
Saccharomyces kudriavzevii |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.8 | 25 | - |
assay at | Saccharomyces cerevisiae |
| 1.1.1.8 | 25 | - |
assay at | Saccharomyces kudriavzevii |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.1.1.8 | 7 | - |
assay at | Saccharomyces cerevisiae |
| 1.1.1.8 | 7 | - |
assay at | Saccharomyces kudriavzevii |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.8 | NAD+ | - |
Saccharomyces cerevisiae | |
| 1.1.1.8 | NAD+ | - |
Saccharomyces kudriavzevii | |
| 1.1.1.8 | NADH | - |
Saccharomyces cerevisiae | |
| 1.1.1.8 | NADH | - |
Saccharomyces kudriavzevii | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 1.1.1.8 | Saccharomyces kudriavzevii | the enzyme shows higher enzymatic activity in response to osmotic and cold stress. The enzyme expression is increased during fermentation | up |
| 1.1.1.8 | Saccharomyces cerevisiae | there is significantly higher enzyme activity after osmotic (2.6, 5.2 and 3.6fold after 2, 4 and 8 h, respectively) and cold stresses (9.7, 19.9 and 2.2fold after 2, 4 and 8 h, respectively) | up |
| 1.1.1.8 | Saccharomyces kudriavzevii | there is significantly higher enzyme activity after osmotic (2.6, 5.2 and 3.6fold after 2, 4 and 8 h, respectively) and cold stresses (9.7, 19.9 and 2.2fold after 2, 4 and 8 h, respectively) | up |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.1.1.8 | evolution | Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7% | Saccharomyces cerevisiae |
| 1.1.1.8 | evolution | Gpd1p from Saccharomyces kudriavzevii presented five conserved amino acid replacements compared to Saccharomyces cerevisiae (Ala31Ile, Ile67leu, Glu76Asp, Asp142Asn and Ser143Pro) out of 391 total residues, corresponding to an identity of 98.7% | Saccharomyces kudriavzevii |
| 1.1.1.8 | metabolism | Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway | Saccharomyces cerevisiae |
| 1.1.1.8 | metabolism | Saccharomyces kudriavzevii has changed the metabolism to promote the branch of the glycolytic pathway involved in glycerol production to adapt to low temperature environments and maintain the NAD+/NADH ratio in alcoholic fermentations. Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway | Saccharomyces kudriavzevii |
| 1.1.1.8 | physiological function | glycerol is increased in Saccharomyces kudriavzevii mainly due to increased Vmax of the Gpd1p enzyme | Saccharomyces kudriavzevii |
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