The synthesis of a novel thio-linked disaccharide of chondroitin as a potential inhibitor of polysaccharide lyases

• Published in: Carbohydrate research Vol. 339; no. 3; pp. 699 - 703
• Main Authors: Rye, Carl S, Withers, Stephen G
• Format: Journal Article
• Language: English
• Published: OXFORD Elsevier Ltd 25.02.2004; Elsevier
• Subjects: Biochemistry & Molecular Biology; Carbohydrate Sequence; Chemistry; Chemistry, Applied; Chemistry, Organic; Chondroitin; Chondroitin - chemical synthesis; Chondroitin - chemistry; Chondroitin - pharmacology; Chondroitin AC; Disaccharides - chemical synthesis; Disaccharides - chemistry; Disaccharides - pharmacology; Flavobacterium - enzymology; Flavobacterium heparinum; Glycosaminoglycan; Kinetics; Life Sciences & Biomedicine; Molecular Structure; Physical Sciences; Polysaccharide lyase; Polysaccharide-Lyases - antagonists & inhibitors; Polysaccharide-Lyases - metabolism; Science & Technology; Sulfhydryl Compounds - chemistry; Glycosaminoglycan; Flavobacterium heparinum; Polysaccharide lyase; Chondroitin AC; Chondroitin; FLAVOBACTERIUM-HEPARINUM; chondroitin AC; MECHANISM; CRYSTAL-STRUCTURE; AC LYASE; ANGSTROM RESOLUTION; chondroitin; polysaccharide lyase; PRODUCT; ENZYMES; DEGRADATION; glycosaminoglycan; A1-III
• ISSN: 0008-6215; 1873-426X
• DOI: 10.1016/j.carres.2003.12.011

Graphic A thio-linked disaccharide based on the structure of the glycosaminoglycan chondroitin was synthesized as a potential inhibitor of chondroitin AC lyase from Flavobacterium heparinum for structural analysis of the active site. Instead it was found to be a slow substrate, thereby demonstrating that lyases, in contrast to glycosidases, can cleave thioglycoside links between sugars.