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Matches in SemOpenAlex for { <https://semopenalex.org/work/W2000493479> ?p ?o ?g. }

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• W2000493479 abstract "The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity." @default.
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• W2000493479 date "2000-12-05" @default.
• W2000493479 modified "2023-10-18" @default.
• W2000493479 title "The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad" @default.
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• W2000493479 doi "https://doi.org/10.1073/pnas.260376797" @default.
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