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3.4.21.B48
evolution
kumamolisin belongs to the family of serine-carboxyl peptidases, i.e. sedolisins
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731647
3.4.21.B48
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one of the reasons for sedolisins to use an aspartate as a catalyst (e.g., Asp164 in kumamolisin) instead of asparagine (the oxyanion-hole residue in classical serine peptidase) might be due in part to the requirement for the creation of a built-in switch that delays the self-activation until secretion into acidic medium. The X-ray structure of the S278A pro-kumamolisin mutant is used to generate the model for the wild-type pro-kumamolisin through a manual change of Ala278 to Ser278
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731647
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