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Chitinases are hydrolytic enzymes that break down glycosidic bonds in chitin. They catalyse the following reaction:
A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
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.
Hurler syndrome, also known as mucopolysaccharidosis Type IH (MPS-IH), Hurler's disease, and formerly gargoylism, is a genetic disorder that results in the buildup of large sugar molecules called glycosaminoglycans (GAGs) in lysosomes. The inability to break down these molecules results in a wide variety of symptoms caused by damage to several different organ systems, including but not limited to the nervous system, skeletal system, eyes, and heart.
Fucoidan is a long chain sulfated polysaccharide found in various species of brown algae. Commercially available fucoidan is commonly extracted from the seaweed species Fucus vesiculosus, Cladosiphon okamuranus, Laminaria japonica and Undaria pinnatifida. Variant forms of fucoidan have also been found in animal species, including the sea cucumber.
Arylsulfatase B is an enzyme associated with mucopolysaccharidosis VI.
Translocase is a general term for a protein that assists in moving another molecule, usually across a cell membrane. These enzymes catalyze the movement of ions or molecules across membranes or their separation within membranes. The reaction is designated as a transfer from “side 1” to “side 2” because the designations “in” and “out”, which had previously been used, can be ambiguous. Translocases are the most common secretion system in Gram positive bacteria.
Heparosan-N-sulfate-glucuronate 5-epimerase is an enzyme with systematic name poly( -beta-D-glucuronosyl- -N-sulfo-alpha-D-glucosaminyl) glucurono-5-epimerase. This enzyme catalyses the following chemical reaction
The enzyme α-L-fucosidase (EC 3.2.1.51) catalyzes the following chemical reaction: an α-L-fucoside + H2O L-fucose + an alcohol
In enzymology, a glycoprotein 6-alpha-L-fucosyltransferase (EC 2.4.1.68) is an enzyme that catalyzes the chemical reaction
In enzymology, a poly(glycerol-phosphate) alpha-glucosyltransferase is an enzyme that catalyzes the chemical reaction
Heparan-α-glucosaminide N-acetyltransferase is an enzyme that in humans is encoded by the HGSNAT gene.
Agarase is an enzyme with systematic name agarose 4-glycanohydrolase. It is found in agarolytic bacteria and is the first enzyme in the agar catabolic pathway. It is responsible for allowing them to use agar as their primary source of carbon and enables their ability to thrive in the ocean.
Porphyran is a sulfated carbohydrate derived from red algae of the genus Porphyra.
κ-Carrageenase is an enzyme with systematic name κ-carrageenan 4-β-D-glycanohydrolase (configuration-retaining). It catalyses the endohydrolysis of (1→4)-β-D-linkages between D-galactose 4-sulfate and 3,6-anhydro-D-galactose in κ-carrageenans
Endogalactosaminidase is an enzyme with systematic name galactosaminoglycan glycanohydrolase. It catalyses endohydrolysis of (1→4)-α-D-galactosaminidic linkages in poly(D-galactosamine).
Iota-carrageenase is an enzyme with systematic name iota-carrageenan 4-beta-D-glycanohydrolase (configuration-inverting). This enzyme catalyses the following chemical reaction
Alpha-agarase is an enzyme with systematic name agarose 3-glycanohydrolase. This enzyme catalyses the following chemical reaction
Beta porphyranase is an enzyme responsible for the degradation of porphyran, which composes the cell wall of red algae. So far only five β-porphyranases have been identified: PorA and PorB are found in the marine bacteria Zobellia galactinovirans. A wild-type porphyranase activity has been found in Pseudoalteromonas atlantica. BpGH16B and BpGH86A have been found in the human gut bacterium, Bacteroides plebeius, of Japanese individuals.
Chondroitin ABC lyase is an enzyme with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction
References
- ↑ Thanassi NM, Nakada HI (1967). "Enzymic degradation of fucoidan by enzymes from the hepatopancreas of abalone, Halotus species". Arch. Biochem. Biophys. 118: 172–177. doi:10.1016/0003-9861(67)90294-9.
