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Caption : fig.s3 sds-page analysis of soluble expression and purification of enzyme. (a) the soluble expression profile of 10 g/l wt enzymes, where 'm' denotes the marker, 's' represents the supernatant, and 'p' indicates the precipitate. (b) the sds-page of the purified enzymes. 'm': the marker. lane 1: wt, lane 2: i192t, lane 3: i201m, lane 4: i205s, lane 5: i192t/i205s, and lane 6: i192t/i201m/i205s. the concentration of each purified protein added is 0.1 mg/ml.

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Caption : fig.s4 the ramachandran plot result.

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Caption : fig.s5 the impact of temperature, ph and substrate concentration to the enzyme activity. (a) optimal temperature, (b) optimal ph, and (c) optimal substrate concentration for both the wt and mutants. the reaction conditions were in consistent with those used for enzyme activity assays. activity was measured in 50 mm potassium phosphate buffer (ph 7.0-8.0), tris-hcl buffer (ph 8.5-9.0) and glycine-naoh buffer (ph 9.5-10.0).

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Caption : fig.s6 the half-life of the wt and mutant enzymes.

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Caption : fig.s7 the kinetic curves of the wt enzyme and the mutant i201m enzyme toward nad+. assay conditions for kinetic resolution: 100 mm potassium phosphate buffer ph 7.5, 5 mm cdca, 0.05-5 mm nad+, approximately 1 mg/ml purified enzyme (dilute 800 times), 30 °c. y axis: activity normalized to μmol yield per minute reaction per mg purified enzyme.