Related Research Articles
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.
Hyaluronidases are a family of enzymes that catalyse the degradation of hyaluronic acid. Karl Meyer classified these enzymes in 1971, into three distinct groups, a scheme based on the enzyme reaction products. The three main types of hyaluronidases are two classes of eukaryotic endoglycosidase hydrolases and a prokaryotic lyase-type of glycosidase.
Hyaluronic acid, also called hyaluronan, is an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. It is unique among glycosaminoglycans as it is non-sulfated, forms in the plasma membrane instead of the Golgi apparatus, and can be very large: human synovial HA averages about 7 million Da per molecule, or about 20,000 disaccharide monomers, while other sources mention 3–4 million Da.
Cystathionine beta-lyase, also commonly referred to as CBL or β-cystathionase, is an enzyme that primarily catalyzes the following α,β-elimination reaction
The enzyme methionine γ-lyase (EC 4.4.1.11, MGL) is in the γ-family of PLP-dependent enzymes. It degrades sulfur-containing amino acids to α-keto acids, ammonia, and thiols:
The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.:
The enzyme ATP-dependent NAD(P)H-hydrate dehydratase catalyzes the chemical reactions
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 glucuronan lyase catalyzes the following process:
The enzyme inulin fructotransferase (DFA-III-forming) catalyzes the following process:
The enzyme pectate disaccharide-lyase catalyzes the following process:
Pectin lyase, also known as pectolyase, is a naturally occurring pectinase, a type of enzyme that degrades pectin. It is produced commercially for the food industry from fungi and used to destroy residual fruit starch, known as pectin, in wine and cider. In plant cell culture, it is used in combination with the enzyme cellulase to generate protoplasts by degrading the plant cell walls.
The enzyme mannuronate-specific alginate lyase catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
The enzyme xanthan lyase catalyzes the following process:
Hyaluronoglucuronidase is an enzyme with systematic name hyaluronate 3-glycanohydrolase. This enzyme catalyses the following chemical reaction
Gellan tetrasaccharide unsaturated glucuronyl hydrolase (EC 3.2.1.179, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp beta-D-4-deoxy-Delta4-GlcAp hydrolase. This enzyme catalyses the following chemical reaction
Gellan lyase is an enzyme with systematic name gellan β-D-glucopyranosyl-(1→4)-D-glucopyranosyluronate lyase. This enzyme catalyses the following process:
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
- Linker A, Hoffman P, Meyer K, Sampson P, Korn ED (1960). "The formation of unsaturated disaccharides from mucopoly-saccharides and their cleavage to alpha-keto acid by bacterial enzymes". Journal of Biological Chemistry. 235: 3061–5. PMID 13762462.
- Meyer K, Rapport MM (1952). "Hyaluronidases". Advances in Enzymology and Related Subjects of Biochemistry. 13: 199–236. PMID 14943668.
- Moran F, Nasuno S, Starr MP (1968). "Extracellular and intracellular polygalalacturonic acid trans-eliminases of Erwinia carotovora". Archives of Biochemistry and Biophysics. 123 (2): 298–306. doi:10.1016/0003-9861(68)90138-0. PMID 5642600.
