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Glycosaminoglycans (GAGs) or mucopolysaccharides are long, linear polysaccharides consisting of repeating disaccharide units. The repeating two-sugar unit consists of a uronic sugar and an amino sugar, except in the case of the sulfated glycosaminoglycan keratan, where, in place of the uronic sugar there is a galactose unit. GAGs are found in vertebrates, invertebrates and bacteria. Because GAGs are highly polar molecules and attract water; the body uses them as lubricants or shock absorbers.
Keratan sulfate (KS), also called keratosulfate, is any of several sulfated glycosaminoglycans that have been found especially in the cornea, cartilage, and bone. It is also synthesized in the central nervous system where it participates both in development and in the glial scar formation following an injury. Keratan sulfates are large, highly hydrated molecules which in joints can act as a cushion to absorb mechanical shock.
Heparinoids are glycosaminoglycans which are chemically and pharmacologically related to heparin. They include oligosaccharides and sulfated polysaccharides of plant, animal, or synthetic origin. Multiple scientific studies have been conducted on heparinoids.
N-acetylgalactosamine-4-sulfatase is an enzyme with systematic name N-acetyl-D-galactosamine-4-sulfate 4-sulfohydrolase. It catalyses the following reaction:
Chondroitinase treatment is a treatment of proteoglycans, a protein in the fluid among cells where they affect neural activity. Chondroitinase treatment has been shown to allow adults vision to be restored as far as ocular dominance is concerned. Moreover, there is some evidence that Chondroitinase could be used for the treatment of spinal injuries.
In enzymology, a chondroitin 4-sulfotransferase is an enzyme that catalyzes the chemical reaction
The enzyme chondroitin AC lyase catalyzes the chemical reaction
The enzyme chondroitin B lyase catalyzes the following process:
The enzyme chondroitin-sulfate-ABC endolyase catalyzes the following process:
The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
The enzyme chondro-6-sulfatase (EC 3.1.6.10) catalyzes the reaction
Carbohydrate sulfotransferase 2 is an enzyme that in humans is encoded by the CHST2 gene.
Carbohydrate sulfotransferase 1 is an enzyme that in humans is encoded by the CHST1 gene.
Carbohydrate sulfotransferase 15 is an enzyme that in humans is encoded by the CHST15 gene. It belongs to the N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase enzyme class.
Dermatan-sulfate epimerase is an enzyme that in humans is encoded by the DSE gene.
Carbohydrate sulfotransferase 12 is an enzyme that in humans is encoded by the CHST12 gene.
Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.
Dermatan 4-sulfotransferase is an enzyme with systematic name 3'-phospho-5'-adenylyl sulfate:(dermatan)-N-acetyl-D-galactosamine 4-sulfotransferase. This enzyme catalyses the following chemical reaction
Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->3)-beta-D-GalNAc6S hydrolase. This enzyme catalyses the following chemical reaction
Chondroitin ABC lyase is an enzyme with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction
References
- Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases and chondrosulfatases". J. Biol. Chem. 243 (7): 1523–35. PMID 5647268.
- Saito H, Yamagata T, Suzuki S (1968). "Enzymatic methods for the determination of small quantities of isomeric chondroitin sulfates". J. Biol. Chem. 243 (7): 1536–42. PMID 4231029.
- Suzuki S, Saito H, Yamagata T, Anno K, Seno N, Kawai Y, Furuhashi T (1968). "Formation of three types of disulfated disaccharides from chondroitin sulfates by chondroitinase digestion". J. Biol. Chem. 243 (7): 1543–50. PMID 5647269.
- Suzuki S; Hashimoto, N; Mochizuki, H; Kato, F; Makiguchi, Y; Horie, K; Suzuki, S (1997). "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially acting on oligosaccharides". J. Biol. Chem. 272 (14): 9123–30. doi: 10.1074/jbc.272.14.9123 . PMID 9083041.
- Lauder RM; Nieduszynski, IA; Giannopoulos, M; Weeks, SD; Sadler, IH; Lauder, RM (2005). "Characterization of oligosaccharides from the chondroitin/dermatan sulfates. 1H-NMR and 13C-NMR studies of reduced trisaccharides and hexasaccharides". FEBS J. 272 (24): 6276–86. doi: 10.1111/j.1742-4658.2005.05009.x . PMID 16336265.
