File S1 - Improving the Secretion of a Methyl Parathion Hydrolase in Pichia pastoris by Modifying Its N-Terminal Sequence

Supporting figures and tables. This file contains Table S1-Table S2 and Figure S1-Figure S6. Table S1, The primers that involved in the construction of the mutants. Table S2, The enzymatic properties of WT and mutant MPH. Figure S1, The sequence alignment of N-terminal of the three proteins. Figure S2, Enzyme activity in culture supernatants (a) and cells (b). Figure S3, The growth kinetics of the selected transformants. Figure S4, SDS/PAGE analysis of the purified WT MPH and mutants (N66-MPH, D10-MPH, N9-MPH). Figure S5, SDS-PAGE analysis of culture supernatants from 72 hours methanol induction. Figure S6, The interaction energy of the protein OPCH2, MPH and N9-MPH. (ZIP)