title: Chondroitin-4-O-sulfatase from Bacteroides thetaiotaomicron: exploration of the substrate specificity.
abstract: Bacterial sulfatases can be good tools to increase the molecular diversity of glycosaminoglycan synthetic fragments. A chondroitin 4-O-sulfatase from the human commensal bacterium Bacteroides thetaiotaomicron has recently been identified and expressed. In order to use this enzyme for synthetic purposes, the minimal structure required for its activity has been determined. For that, four 4-O-sulfated monosaccharides and one 4-O-sulfated disaccharide have been synthesized and used as substrates with the sulfatase. The minimum structure was shown to be a disaccharide but in contrast to the natural substrate, which must have a 4,5-insaturation, the enzyme accepts as substrate, a disaccharide with a saturated glucuronic acid at the non-reducing end and even a glucopyranosyl moiety without the carboxylic acid functionality.
authors.affiliation: Univ Paris-Sud and CNRS, LCOM-eG2M, Institut de Chimie Moléculaire et des Matériaux d'Orsay, CNRS UMR 8182, LabEx LERMIT, Bât 420, Orsay F-91405, France.
authors.forename: Annie
authors.initials: A
authors.lastname: Malleron
authors.forename: Alhosna
authors.initials: A
authors.lastname: Benjdia
authors.forename: Olivier
authors.initials: O
authors.lastname: Berteau
authors.forename: Christine
authors.initials: C
authors.lastname: Le Narvor
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D001439:Bacteroides / Q000201:enzymology*; D015394:Molecular Structure; D009005:Monosaccharides / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D013429:Sulfatases / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D009005:Monosaccharides; D013429:Sulfatases