Molecular basis for acceptor substrate specificity of the human β1,3-glucuronosyltransferases GlcAT-I and GlcAT-P involved in glycosaminoglycan and HNK-1 carbohydrate epitope biosynthesis, respectively

Autor: Rafael Oriol, Jacques Magdalou, Sylvie Fournel-Gigleux, Patrick Netter, Guillermo Mulliert, Sandrine Gulberti, Magali Fondeur-Gelinotte, Virginie Lattard, Michael W.H. Coughtrie, Mohamed Ouzzine

Publikováno v: Glycobiology. 17:857-867

The human beta1,3-glucuronosyltransferases galactose-beta1,3-glucuronosyltransferase I (GlcAT-I) and galactose-beta1,3-glucuronosyltransferase P (GlcAT-P) are key enzymes involved in proteoglycan and HNK-1 carbohydrate epitope synthesis, respectively

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea31c1711df6be2f37193b0c0fc73340
https://doi.org/10.1093/glycob/cwm055

PuriWcation and characterization of a soluble form of the recombinant human galactose-1,3-glucuronosyltransferase I expressed in the yeast Pichia pastoris

Autor: Jacques Magdalou, Magali Fondeur-Gelinotte, Sylvie Fournel-Gigleux, Joseph Boudrant, Sandrine Gulberti, Patrick Netter, Virginie Lattard, Mohamed Ouzzine, Jean-Claude Jacquinet

Publikováno v: Protein Expression and Purification
Protein Expression and Purification, Elsevier, 2006, 47 (Issue 1), pp.137-143. ⟨10.1016/j.pep.2005.10.012⟩

The galactose-beta1,3-glucuronosyltransferase I (GlcAT-I) catalyzes the transfer of glucuronic acid from UDP-alpha-D-glucuronic acid onto the terminal galactose of the trisaccharide glycosaminoglycan-protein linker region of proteoglycans. This enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64001d8f2b22cfa00dfed0a180774143
https://hal.archives-ouvertes.fr/hal-00287724