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Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases
C Breton1, E Bettler, D H Joziasse
1Centre de Recherches sur les Macromolécules Végétales,Vrije Universiteit, Amsterdam, The Netherlands. breton@cermav.cnrs.fr
Journal of Biochemistry
|May 30, 1998
Summary
Galactosyltransferases are enzymes that transfer galactose. Sequence analysis classified these enzymes into twelve groups and defined five conserved structural families, revealing a key DxD motif in most.
Area of Science:
- Biochemistry
- Enzymology
- Glycobiology
Background:
- Galactosyltransferases catalyze the transfer of galactose from UDP-Gal to acceptors.
- These enzymes form various glycosidic linkages, including alpha and beta configurations.
- Recent availability of cDNA sequences has enabled detailed enzymatic studies.
Purpose of the Study:
- To classify galactosyltransferases based on sequence similarity and catalytic function.
- To identify conserved structural features and define enzyme families.
- To investigate the presence and significance of the DxD motif.
Main Methods:
- Retrieval and analysis of galactosyltransferase cDNA sequences.
- Sequence similarity studies and protein comparison using graphics methods.
- Identification of conserved regions and invariant residues.
Main Results:
- Galactosyltransferases were classified into twelve groups based on reaction and sequence identity.
- Five conserved structural families were defined across galactosyltransferases and other glycosyltransferases.
- Conserved regions, invariant residues, and the DxD motif were identified in most families.
Conclusions:
- Sequence analysis provides a robust framework for galactosyltransferase classification.
- Conserved structural features suggest evolutionary relationships among glycosyltransferases.
- The DxD motif is a potentially critical element for enzyme function across multiple families.