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Fig. 6 | Microbial Cell Factories

Fig. 6

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

Fig. 6

Structural models of IDI (a) and the mutation location: (b) L141; (c) L141H. a The location sites of the beneficial mutations were marked and the active site catalytic triad residues were marked in green. b Catalytic residues of activity pocket (His-93, His-104, Cys-139, Glu-205, Glu-207, Mg-302 and Mg-400) were marked respectively. c L141H substitution showed His-141 participated in the construction of the active pocket, which enlarged the IDI catalytic domain

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