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Fig. 7 | Microbial Cell Factories

Fig. 7

From: Enhancement of the catalytic activity of Isopentenyl diphosphate isomerase (IDI) from Saccharomyces cerevisiae through random and site-directed mutagenesis

Fig. 7

Structural models of mutation locations: a L141; b L141H; c Y195, W256; d Y195F, W256C. a, b L141H substitution showed His-141 formed a hydrogen bond with β-phosphates of IPP, strengthening binding of IPP. c, d Phe-195 and Cys-256 substitution was located near the hydrophobic group of IPP and improved the stability of binding of IPP

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