J. Biochem, 1998, Vol. 123, No. 6 1000-1009
© 1998 Japanese Biochemical Society
review-article |
Sequence-Function Relationships of Prokaryotic and Eukaryotic Galactosyltransferases1
*Centre de Recherches sur les Macromolécules Végétales3 CNRS BP 53, F-38041 Grenoble cedex 9, France
Department of Medical Chemistry, Vrije Universiteit Van der Boechorststraat 7, 1081 BT Amsterdam, The Netherlands
2To whom correspondence should be addressed. Tel: +33 4 76 03 76 35, Fax: +33 4 76 54 72 03, E-mail: breton{at}cermav.cnrs.fr
Galactosyltransferases are enzymes which transfer galactose from UDP-Gal to various acceptors with either retention of the anomeric configuration to form 
1,2-,1,3-,1,4-,and 1,6-linkages, or inversion of the anomeric configuration to form ß1,3-, ß1,4-, and ß1-ceramide linkages. During the last few years, several (c)DNA sequences coding for galactosyltransferases became available. We have retrieved these sequences and conducted sequence similarity studies. On the basis of both the nature of the reaction catalyzed and the protein sequence identity, these enzymes can be classified into twelve groups. Using a sensitive graphics method for protein comparison, conserved structural features were found in some of the galactosyltransferase groups, and other classes of glycosyltransferases, resulting in the definition of five families. The lengths and locations of the conserved regions as well as the invariant residues are described for each family. In addition, the DxD motif that may be important for substrate recognition and/or catalysis is demonstrated to occur in all families but one.
1 This work was supported by the following grants: Programme Physique et Chimie du Vivant-CNRS, Immunology Concerted Action 3026PL950004, and Xenotransplantation Project BIO4CT972242 of the BIOTECH program from the European Union.
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