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Literature summary for 1.1.1.8 extracted from

  • Oliveira, B.M.; Barrio, E.; Querol, A.; Perez-Torrado, R.
    Enhanced enzymatic activity of glycerol-3-phosphate dehydrogenase from the cryophilic Saccharomyces kudriavzevii (2014), PLoS ONE, 9, e87290.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme shows higher enzymatic activity in response to osmotic and cold stress Saccharomyces kudriavzevii

Application

Application Comment Organism
food industry potential use of Saccharomyces cerevisiae-Saccharomyces kudriavzevii hybrids in the wine industry where glycerol content is an important quality parameter Saccharomyces cerevisiae
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)

Cloned (Comment) Organism
gene GPD1, quantitative real-time PCR expression analysis Saccharomyces cerevisiae
gene GPD1, quantitative real-time PCR expression analysis Saccharomyces kudriavzevii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.051
-
NADH at pH 7.0 and 25°C Saccharomyces cerevisiae
0.11
-
NADH at pH 7.0 and 25°C Saccharomyces kudriavzevii
0.54
-
dihydroxyacetone phosphate at pH 7.0 and 25°C Saccharomyces cerevisiae
0.61
-
dihydroxyacetone phosphate at pH 7.0 and 25°C Saccharomyces kudriavzevii

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Saccharomyces cerevisiae 5737
-
cytoplasm
-
Saccharomyces kudriavzevii 5737
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sn-glycerol 3-phosphate + NAD+ Saccharomyces cerevisiae
-
glycerone phosphate + NADH + H+
-
r
sn-glycerol 3-phosphate + NAD+ Saccharomyces kudriavzevii
-
glycerone phosphate + NADH + H+
-
r

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-
Saccharomyces cerevisiae Q00055 strain S288c; several strains
-
Saccharomyces cerevisiae BY4741
-
-
-
Saccharomyces kudriavzevii
-
-
-
Saccharomyces kudriavzevii A0A060KZ16 several strains
-
Saccharomyces kudriavzevii IFO1802
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information glycerol production rates of different strains, overview Saccharomyces cerevisiae
-
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroxyacetone phosphate + NADH + H+
-
Saccharomyces cerevisiae sn-glycerol 3-phosphate + NAD+
-
?
dihydroxyacetone phosphate + NADH + H+
-
Saccharomyces kudriavzevii sn-glycerol 3-phosphate + NAD+
-
?
dihydroxyacetone phosphate + NADH + H+
-
Saccharomyces cerevisiae BY4741 sn-glycerol 3-phosphate + NAD+
-
?
dihydroxyacetone phosphate + NADH + H+
-
Saccharomyces kudriavzevii IFO1802 sn-glycerol 3-phosphate + NAD+
-
?
sn-glycerol 3-phosphate + NAD+
-
Saccharomyces cerevisiae glycerone phosphate + NADH + H+
-
r
sn-glycerol 3-phosphate + NAD+
-
Saccharomyces kudriavzevii glycerone phosphate + NADH + H+
-
r

Synonyms

Synonyms Comment Organism
GPD1
-
Saccharomyces cerevisiae
GPD1
-
Saccharomyces kudriavzevii
Gpd1p
-
Saccharomyces cerevisiae
Gpd1p
-
Saccharomyces kudriavzevii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae
25
-
assay at Saccharomyces kudriavzevii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Saccharomyces cerevisiae
7
-
assay at Saccharomyces kudriavzevii

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Saccharomyces cerevisiae
NAD+
-
Saccharomyces kudriavzevii
NADH
-
Saccharomyces cerevisiae
NADH
-
Saccharomyces kudriavzevii

Expression

Organism Comment Expression
Saccharomyces kudriavzevii the enzyme shows higher enzymatic activity in response to osmotic and cold stress. The enzyme expression is increased during fermentation up
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
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

General Information Comment Organism
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
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
metabolism Gpd1p is the flux controlling enzyme in the glycerol biosynthetic pathway Saccharomyces cerevisiae
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
physiological function glycerol is increased in Saccharomyces kudriavzevii mainly due to increased Vmax of the Gpd1p enzyme Saccharomyces kudriavzevii