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Phylogenetic and mutational analyses reveal key residues for UDP-glucuronic acid binding and activity of beta1,3-glucuronosyltransferase I (GlcAT-I).

Protein science : a publication of the Protein Society - 1 Jul 2006

Fondeur-Gelinotte Magali, Lattard Virginie, Oriol Rafael, Mollicone Rosella, Jacquinet Jean-Claude, Mulliert Guillermo, Gulberti Sandrine, Netter Patrick, Magdalou Jacques, Ouzzine Mohamed, Fournel-Gigleux Sylvie

Abstract excerpt

The beta1,3-glucuronosyltransferases are responsible for the completion of the protein-glycosaminoglycan linkage region of proteoglycans and of the HNK1 epitope of glycoproteins and glycolipids by transferring glucuronic acid from UDP-alpha-D-glucuronic acid (UDP-GlcA) onto a terminal galactose residue. Here, we develop phylogenetic and mutational approaches to identify critical residues involved in UDP-GlcA...

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Amino Acids
Binding Sites
Conserved Sequence
Glucuronosyltransferase

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PMID: 16815917
DOI: 10.1110/ps.062089106
PMCID: PMC2242556

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