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Literature summary for 2.4.1.40 extracted from

  • Fluegge, F.; Peters, T.
    Insights into allosteric control of human blood group A and B glycosyltransferases from dynamic NMR (2019), ChemistryOpen, 8, 760-769 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
Methyl-TROSY-based titration experiments in combination with zz-exchange experiments show dramatic changes of binding kinetics associated with allosteric interactions between donor-type and acceptor-type ligands. Binding of the acceptor substrates H-disaccharide, H-type II trisaccharide, and H-type VI trisaccharide affects the chemical shifts of the 13C-methyl groups of Met 266, Val 299, Leu 324, and Leu 329, which belong to the acceptor substrate binding pocket. Depending on substrate concentrations in the Golgi apparatus an acceptor route and a donor route are possible. At high local concentrations of UDP-Gal or UDP-GalNAc binding of the nucleotide sugar to GTB or GTA would precede binding of the H-antigen. At low nucleotide sugar concentrations, it can be assumed that H-antigen binds first. In this latter case, the enzymes may discriminate between different types of H-antigens, preferring e. g. type-II over type-I H-antigens Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P16442
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