Crystal structure of α-1,3-galactosyltransferase (α3GT) in a complex with p-nitrophenyl-β-galactoside (pNPβGal)

H Jamaluddin, P Tumbale, T A Ferns, N Thiyagarajan, K Brew, K Ravi Acharya

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The specificities of glycosyltransferases make them useful for the synthesis of biologically active oligosaccharides, but also restrict their range of products. In substrate engineering, substrate promiscuity is enhanced by attaching removable interactive groups to weak substrates. Thus, the attachment of β p-nitrophenyl converts galactose from a poor into a good substrate of α-1,3-galactosyltransferase. The crystallographic structure of a complex of α3GT containing p-nitrophenyl-β-galactoside shows that the p-nitrophenyl binds similarly to the N-acetylglucosamine of the substrate, N-acetyllactosamine, interacting with the indole of Trp249. p-Nitrophenyl, unlike N-acetylglucosamine, makes no H-bonds but has more non-polar interactions, making it an effective monosaccharide mimetic.
Original languageEnglish
Pages (from-to)601-604
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume385
Issue number4
DOIs
Publication statusPublished - 7 Aug 2009

Keywords

  • α-1
  • Crystal structure
  • Substrate binding
  • Enzyme kinetics
  • 3-Galactosyltransferase
  • Glycosyltransferase

Fingerprint Dive into the research topics of 'Crystal structure of α-1,3-galactosyltransferase (α3GT) in a complex with p-nitrophenyl-β-galactoside (pNPβGal)'. Together they form a unique fingerprint.

  • Cite this