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Literature summary for 1.2.1.12 extracted from

  • Linck, A.; Vu, X.K.; Essl, C.; Hiesl, C.; Boles, E.; Oreb, M.
    On the role of GAPDH isoenzymes during pentose fermentation in engineered Saccharomyces cerevisiae (2014), FEMS Yeast Res., 14, 389-398.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information a downregulation of GAPDH activity does not contribute to improved performance of engineered Saccharomyces cerevisiae on pentose substrates Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.25
-
D-glyceraldehyde 3-phosphate isoform TDH3, pH 8.5, 25°C Saccharomyces cerevisiae
0.42
-
D-glyceraldehyde 3-phosphate isoform TDH2, pH 8.5, 25°C Saccharomyces cerevisiae
0.86
-
D-glyceraldehyde 3-phosphate isoform TDH1, pH 8.5, 25°C Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Saccharomyces cerevisiae 3-phospho-D-glyceroyl phosphate + NADH
-
r

Synonyms

Synonyms Comment Organism
TDH1
-
Saccharomyces cerevisiae
TDH2
-
Saccharomyces cerevisiae
TDH3
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9.1
-
D-glyceraldehyde 3-phosphate isoform TDH3, pH 8.5, 25°C Saccharomyces cerevisiae
16
-
D-glyceraldehyde 3-phosphate isoform TDH2, pH 8.5, 25°C Saccharomyces cerevisiae
29
-
D-glyceraldehyde 3-phosphate isoform TDH1, pH 8.5, 25°C Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function deletion mutants of isoforms TDH1, TDH2, TDH3 show decreased enzymic activity following the trend ?tdh3>?tdh2>?tdh1 in both YEPD or YEPE medium. TDH3 encodes the major GAPDH isoenzyme. The GAPDH total activity is significantly lower in all genotypes grown on ethanol in comparison with the activity on glucose. A downregulation of GAPDH activity does not contribute to improved performance of engineered Saccharomyces cerevisiae on pentose substrates Saccharomyces cerevisiae