Glycine → (R)-2-Octanol

Participants

Reaction Steps

Then, we examined 4-chloroacetoacetic acid ethyl ester reductase activity of the enzyme obtained from Example 3 changing pH by using phosphate buffer (KPB), Tris-HCl buffer, and Glycine buffer. FIG. 2 shows relative activity with taking the maximal activity as 100. As a result, the optimum pH of the enzyme was from 5.0 to 6.5.

Provenance & Evidence