Trends in Glycoscience and Glycotechnology
Online ISSN : 1883-2113
Print ISSN : 0915-7352
ISSN-L : 0915-7352
Crystal Structure-Based Analysis of Human Glucuronyltransferase 1
Lars C. PedersenThomas A. DardenYoshimitsu KakutaMasahiko Negishi
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2001 Volume 13 Issue 70 Pages 121-129

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Abstract
Glucuronyltransferase I (GIcAT-I) is a key enzyme in heparan/chondroitin biosynthesis (1). The X-ray crystal structure of human GlcAT-1 has been solved in the presence of both UDP and substrate analog. The structure reveals a two subdomain structure known as the SGC domain. Donor substratebinding site resides in the N-terminal sub-domain, while acceptor substrate-binding site is located in the C-terminal sub-domain. In addition to conserved residues responsible for the donor binding, various residues that interact with the acceptor molecule have now been identified. The GlcAT-1 provides the structural basis for understanding the structure and function of glycosyltransferases.
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