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Fig. 2 | Microbial Cell Factories

Fig. 2

From: Structure-guided engineering of α-ketoisocaproate dioxygenase increases isobutene production in Synechocystis sp. PCC 6803

Fig. 2

Sequence and structural analysis of HPPD enzymes. A. Alignment of RnKICD amino acid sequence with selected sequences of HPPD enzymes from various species and consensus logos showing the conservation within each position. Sections not relevant to this study are omitted for clarity. Normalized consensus logos were generated in Jalview based on the 262 sequences used for multiple sequence alignment. B. Homology model of the RnKICD active site in open conformation with HPP as substrate. C. Homology model of the RnKICD active site in closed conformation with HPP as substrate. D. Homology model of the RnKICD active site in open conformation with KIC as substrate. E. Homology model of the RnKICD active site in closed conformation with KIC as substrate. Rational design targets are highlighted in yellow, and the site-saturation targets in pink. The structure of HPP is shown in light blue, and the structure of KIC in green. The iron atom is represented by an orange sphere

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Microbial Cell Factories

ISSN: 1475-2859

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