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Heparin, also known as unfractionated heparin (UFH), is a medication and naturally occurring glycosaminoglycan. Since heparins depend on the activity of antithrombin, they are considered anticoagulants. Specifically it is also used in the treatment of heart attacks and unstable angina. It is given intravenously or by injection under the skin. Other uses for its anticoagulant properties include inside blood specimen test tubes and kidney dialysis machines.
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.
Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. It occurs as a proteoglycan in which two or three HS chains are attached in close proximity to cell surface or extracellular matrix proteins. In this form, HS binds to a variety of protein ligands, including Wnt, and regulates a wide range of biological activities, including developmental processes, angiogenesis, blood coagulation, abolishing detachment activity by GrB, and tumour metastasis. HS has also been shown to serve as cellular receptor for a number of viruses, including the respiratory syncytial virus. One study suggests that cellular heparan sulfate has a role in SARS-CoV-2 Infection, particularly when the virus attaches with ACE2.
N-acetylgalactosamine-6-sulfatase is an enzyme that, in humans, is encoded by the GALNS gene.
Flavobacterium columnare is a thin Gram-negative rod bacterium of the genus Flavobacterium. The name derives from the way in which the organism grows in rhizoid columnar formations.
The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction
The enzyme D-dopachrome decarboxylase (EC 4.1.1.84) 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 chondroitin-sulfate-ABC exolyase catalyzes the following process:
The enzyme oligogalacturonide lyase catalyzes the chemical reaction
Pectin lyase is a polysaccharide enzyme with a complex structure that is present in plant cell walls. It has a significant role in pectin degradation and different biotechnological and industrial applications. It can be found in different organisms.
In enzymology, a pinene synthase is an enzyme that catalyzes the chemical reaction
The enzyme mannuronate-specific alginate lyase catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
The enzyme N-acetylgalactosamine-6-sulfatase catalyzes the chemical reaction of cleaving off the 6-sulfate groups of the N-acetyl-D-galactosamine 6-sulfate units of the macromolecule chondroitin sulfate and, similarly, of the D-galactose 6-sulfate units of the macromolecule keratan sulfate.
Sulfotransferase 1A3/1A4 is an enzyme that in humans is encoded by the SULT1A3 gene.
(S)-hydroxynitrile lyase (EC 4.1.2.47, (S)-cyanohydrin producing hydroxynitrile lyase, (S)-oxynitrilase, (S)-HbHNL, (S)-MeHNL, hydroxynitrile lyase, oxynitrilase, HbHNL, MeHNL, (S)-selective hydroxynitrile lyase, (S)-cyanohydrin carbonyl-lyase (cyanide forming), hydroxynitrilase) is an enzyme with systematic name (S)-cyanohydrin lyase (cyanide forming). This enzyme catalyses the interconversion between cyanohydrins and the carbonyl compounds derived from the cyanohydrin with free cyanide, as in the following two chemical reactions:
Chondroitin ABC lyase is an enzyme with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction
Ulvan lyase is an enzyme found within the cell-wall of the marine organism Ulvales, and some marine bacterium. A lyase is a class of enzyme that catalyzes the breakdown of chemical bonds through an elimination reaction mechanism, rather than a substitution reaction mechanism. Ulvan lyase belongs to the polysaccharide lyase family, a type of enzyme that primarily functions to cleave glycosidic linkages in polysaccharides.
References
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- Pojasek K, Shriver Z, Kiley P, Venkataraman G, Sasisekharan R (2001). "Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum". Biochem. Biophys. Res. Commun. 286 (2): 343–51. doi:10.1006/bbrc.2001.5380. PMID 11500043.
- Cygler M; Shilton, BH; Li, Y; Allaire, M; Laliberté, M; Eggimann, B; Cygler, M (1998). "Crystallization and preliminary analysis of chondroitinase AC from Flavobacterium heparinum". Acta Crystallogr. D . 54 (Pt 2): 279–80. doi:10.1107/S0907444997009037. PMID 9761894.
- 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. S2CID 40325628.
