Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase.

@article{Zhang2004RolesOA,
  title={Roles of active site tryptophans in substrate binding and catalysis by alpha-1,3 galactosyltransferase.},
  author={Yingnan Zhang and Ashlesha Deshpande and Zhihong Xie and Ramanathan Natesh and K. Ravi Acharya and Keith Brew},
  journal={Glycobiology},
  year={2004},
  volume={14 12},
  pages={
          1295-302
        }
}
Aromatic amino acids are frequent components of the carbohydrate binding sites of lectins and enzymes. Previous structural studies have shown that in alpha-1,3 galactosyltransferase, the binding site for disaccharide acceptor substrates is encircled by four tryptophans, residues 249, 250, 314, and 356. To investigate their roles in enzyme specificity and catalysis, we expressed and characterized variants of the catalytic domain of alpha-1,3 galactosyltransferase with substitutions for each… CONTINUE READING

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SHOWING 1-10 OF 30 REFERENCES

SHELXL: high-resolution refinement.

  • Methods in enzymology
  • 1997
VIEW 2 EXCERPTS
HIGHLY INFLUENTIAL

Identification and characterization of an UDP-gal: N-acetyllactosaminide a1,3-D-galactosyltransferase in calf thymus

D. H. van den Eijnden, W. M. Blanken, H. Winterwerp, Schiphorst, W.E.C.M
  • Eur J. Biochem.,
  • 1983
VIEW 1 EXCERPT
HIGHLY INFLUENTIAL

Mole - cular modeling of glycosyltransferases involved in the biosynthesis of blood group A , blood group B , Forssman , and igb 3 antigens and their interaction with substrates

C. Breton, Moravcov a, A. Imberty
  • Glycobiology
  • 2003

Molecular modeling of glycosyltransferases involved in the biosynthesis

A. Imberty
  • 2003