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shine815金虫 (正式写手)
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Consequently, after improvement of the wild-type HNL acting on its natural substrate, Glieder et al. tailored the enzyme for (R)-2-chloromandelonitrile production by means of in silico methods and site-directed mutagenesis. Molecular docking simulations in the active site of a homology model of PaHNL5 based on the structure of the homologous isoenzyme PaHNL1 enabled the elucidation of unfavorable steric interactions of the o-chloro substituent and amino acid residues in the catalytic center, particularly alanine 111. Molecular modeling studies revealed a similar binding mode for (S)-2-nitro-1-phenylethanol in the catalytic center of HbHNL as it was determined experimentally for (S)-mandelonitrile, preserving all mechanistically important polar interactions with active-site residues. |
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shine815
金虫 (正式写手)
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2楼2009-02-12 08:08:11
shine815
金虫 (正式写手)
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3楼2009-02-17 09:43:59
