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Catalytic Triads and Their Relatives

  1. Author:
    Dodson, G.
    Wlodawer, A.

  2. Author Address

    Dodson G UNIV YORK DEPT CHEM YORK YO10 5DD N YORKSHIRE ENGLAND NATL INST MED RES LONDON NW7 1AA ENGLAND NCI FREDERICK CANC RES & DEV CTR ABL BASIC RES PROGRAM FREDERICK, MD 21702 USA
    1. Year: 1998
  2. Journal: Trends in Biochemical Sciences
    1. 23
    2. 9
    3. Pages: 347-352
  4. Type of Article: Review
  1. Abstract:

    Interactions among the residues in the serine protease Asp-His-Ser catalytic triad, in the special environment of the enzyme-substrate complex, activate the nucleophilic potential of the seryl Oy. In the subtilisin and trypsin families, the composition and arrangement of the catalytic triad do not vary significantly. However, the mechanisms of action of many other hydrolytic enzymes, which target a wide range of substrates, involve nucleophilic attack by a serine (or threonine) residue. Review of these enzymes shows that the acid-base-ser/thr pattern of catalytic residues is generally conserved, although the individual acids and bases can vary. The variations in sequence and organization illustrate the adaptability shown by proteins in generating catalytic stereochemistry on different main-chain frameworks. [References: 41]

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