Molecular Recognition of UDP-Gal by β-1,4-Galactosyltransferase T1

Thorsten Biet; Thomas Peters

doi:10.1002/1521-3773(20011119)40:22<4189::AID-ANIE4189>3.0.CO;2-A

Molecular Recognition of UDP-Gal by β-1,4-Galactosyltransferase T1

Angew Chem Int Ed Engl. 2001 Nov 19;40(22):4189-4192. doi: 10.1002/1521-3773(20011119)40:22<4189::AID-ANIE4189>3.0.CO;2-A.

Authors

Thorsten Biet¹, Thomas Peters¹

Affiliation

¹ Institut für Chemie, Medizinische Universität zu Lübeck Ratzeburger Allee 160, 23538 Lübeck, Germany, Fax: (+49) 451-500-4241.

PMID: 29712080
DOI: 10.1002/1521-3773(20011119)40:22<4189::AID-ANIE4189>3.0.CO;2-A

Abstract

Saturation transfer difference (STD) NMR experiments reveal the binding epitopes of UDP-Gal and UDP-Glc bound to the glycosyltransferase β4Gal-T1. 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 β4Gal-T1 binds to UDP-Glc but is unable to transfer glucose to an acceptor substrate.

Keywords: NMR spectroscopy; carbohydrates; glycoproteins; molecular recognition; transferases.