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Literature summary for 2.4.1.40 extracted from

  • Grimm, L.; Weissbach, S.; Fluegge, F.; Begemann, N.; Palcic, M.; Peters, T.
    Protein NMR studies of substrate binding to human blood group A and B glycosyltransferases (2017), ChemBioChem, 18, 1260-1269 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme adopts an open conformation in the absence of substrates. Binding of UDP induces a semiclosed conformation. In the presence of both donor and acceptor substrates, the enzymes shift towards a closed conformation with ordering of an internal loop and the C-terminal residues, which then completely cover the donor-binding pocket. The enzyme shows substantial plasticity and conformational flexibility. Residues Ile123 at the bottom of the UDP binding pocket, and Ile192 as part of the internal loop are significantly disturbed upon stepwise addition of UDP and H-disaccharide-O-CH3 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P16442
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