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Fig. 5 | Microbial Cell Factories

Fig. 5

From: Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium

Fig. 5

Effects of mutation on SfSFGH enzymatic activity. a Comparison of relative activities between wild-type SfSFGH and several point mutants (L55A, L55 V, H147A, W182A, and F226A). All mutants are located on the substrate-binding pocket. Assays were carried out using various substrates (p-NA, p-NB, p-NH, p-NO, p-NDe, p-NDo, and p-NPP). The relative activity of wild-type SfSFGH with p-NA was set to 100%. b Increased enzymatic activity for α-NB in the W182A mutant was observed compared with that of wild-type SfSFGH. The relative activity of wild-type SfSFGH with α-NA was set to 100%. c The surface of the substrate-binding site of SfSFGH is colored grey. The catalytic triad residues (Ser148, Asp224, and His257; salmon) and Trp182 (cyan) are presented as a stick model. d Hydrolytic activities towards α-d-glucose penta-acetate, cellulose acetate, and N-acetyl-d-glucosamine. All experiments were performed in triplicate

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