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  • OER000002930.pdf.jpg
  • Journal article

  • Cooperativity of catalytic and lectin-like domain of T. congolense trans-sialidase modulates its catalytic activity

    • Authors : Waespy, Mario (2021)

  • Trans-sialidases (TS) represent a multi-gene family of unusual enzymes, which catalyse the transfer of terminal sialic acids from sialoglycoconjugates to terminal galactose or N 30 acetylgalactosamine residues of oligosaccharides without the requirement of CMP-Neu5Ac, the activated Sia used by typical sialyltransferases. Most work on trypanosomal TS has been done on enzymatic activities of TS from T. cruzi (causing Chagas disease in Latin America), s...
  • OER000002435.pdf.jpg
  • Ebooks (Sách điện tử)

  • Understanding ATP binding to DosS catalytic domain with a short ATP-lid

    • Authors : Larson, Grant  (2023)

  • DosS is a heme-sensor histidine kinase that responds to redox-active stimuli in mycobacterial environments by triggering dormancy transformation. Sequence comparison of the catalytic ATP-binding (CA) domain of DosS to other well-studied histidine kinases suggests that it possesses a rather short ATP-lid. This feature has been thought to inhibit DosS kinase activity by blocking ATP binding in the absence of interdomain interactions with the dimerization and histidi...