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Table 4 Substrates specificity of ER10 and ER25 enzymes

From: Identification, characterization of two NADPH-dependent erythrose reductases in the yeast Yarrowia lipolytica and improvement of erythritol productivity using metabolic engineering

Substrates ER10a Reductase activity (U/mg protein)
ER10b ER25a ER25b
d-Erythrose 8.2 (100) 8.3 (100) 14.6 (100) 14.1 (100)
l-Arabinose 4.3 (52.4) 4.1 (49.4) 1.8 (12.3) 1.5 (10.6)
d-Xylose 2.4 (29.3) 2.5 (30.1) ND ND
d-Ribose 3.4 (41.5) 3.1 (37.3) ND ND
d-Xylulose 1.3 (15.9) 1.1 (13.3) ND ND
  1. ND no activity detected. (Relative activity compared to d-erythrose). The values provided are the means of three independent replicates; the standard deviations represented less than 10% of the means
  2. aActivity determined in 50 mM phosphate buffer at its optimal pH (pH 6 for ER10, and pH 4 for ER25)
  3. bActivity determined in 50 mM phosphate buffer with high osmotic condition (200 g/L glucose) at its optimal pH