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Molecular Recognition of UDP‐Gal by β ‐1,4‐Galactosyltransferase T1
Author(s) -
Biet Thorsten,
Peters Thomas
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20011119)40:22<4189::aid-anie4189>3.0.co;2-a
Subject(s) - galactosyltransferase , glycosyltransferase , residue (chemistry) , chemistry , acceptor , galactose , enzyme , epitope , stereochemistry , biochemistry , biology , physics , genetics , antibody , condensed matter physics
Saturation transfer difference (STD) NMR experiments reveal the binding epitopes of UDP‐Gal and UDP‐Glc bound to the glycosyltransferase β 4Gal‐T1 (see picture). Whereas the enzyme recognizes the galactose residue in UDP‐Gal, it does not make any close contacts with the glucose residue in UDP‐Glc. This observation explains why β 4Gal‐T1 binds to UDP‐Glc but is unable to transfer glucose to an acceptor substrate.