The catalytic triad of serine peptidases

@article{Polgr2005TheCT,
  title={The catalytic triad of serine peptidases},
  author={L. Polg{\'a}r},
  journal={Cellular and Molecular Life Sciences CMLS},
  year={2005},
  volume={62},
  pages={2161-2172}
}
  • L. Polgár
  • Published 2005
  • Biology, Medicine
  • Cellular and Molecular Life Sciences CMLS
  • Abstract.The catalytic action of serine peptidases depends on the interplay of a nucleophile, a general base and an acid. In the classic trypsin and subtilisin families this catalytic triad is composed of serine, histidine and aspartic acid residues and exhibits similar spatial arrangements, but the order of the residues in the amino acid sequence is different. By now several new families have been discovered, in which the nucleophile-base-acid pattern is generally conserved, but the individual… CONTINUE READING
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    References

    SHOWING 1-10 OF 130 REFERENCES
    Catalytic triads and their relatives.
    • 544
    Dissecting the catalytic triad of a serine protease
    • 494
    • PDF
    Catalytic hydroxyl/amine dyads within serine proteases.
    • 123
    The chemistry and enzymology of the type I signal peptidases
    • 259
    Serine protease mechanism and specificity.
    • 1,296
    • PDF