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Tryptophan synthase or tryptophan synthetase is an enzyme that catalyzes the final two steps in the biosynthesis of tryptophan. It is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae. However, it is absent from Animalia. It is typically found as an α2β2 tetramer. The α subunits catalyze the reversible formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunits catalyze the irreversible condensation of indole and serine to form tryptophan in a pyridoxal phosphate (PLP) dependent reaction. Each α active site is connected to a β active site by a 25 Ångstrom long hydrophobic channel contained within the enzyme. This facilitates the diffusion of indole formed at α active sites directly to β active sites in a process known as substrate channeling. The active sites of tryptophan synthase are allosterically coupled.
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 MDa per molecule, or about 20,000 disaccharide monomers, while other sources mention 3–4 MDa.
β-Amylase is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It catalyses the following reaction:
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 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 inulin fructotransferase (DFA-III-forming) catalyzes the following process:
The enzyme mannuronate-specific alginate lyase catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
In enzymology, a [acyl-carrier-protein] S-acetyltransferase is an enzyme that catalyzes the reversible chemical reaction
In enzymology, an amylosucrase is an enzyme that catalyzes the chemical reaction
In enzymology, a 4-alpha-glucanotransferase is an enzyme that catalyzes a chemical reaction that transfers a segment of a 1,4-alpha-D-glucan to a new position in an acceptor carbohydrate, which may be glucose or a 1,4-alpha-D-glucan.
In enzymology, a cyclomaltodextrin glucanotransferase is an enzyme that catalyzes the chemical reaction of cyclizing part of a 1,4-alpha-D-glucan molecule through the formation of a 1,4-alpha-D-glucosidic bond. They are bacterial enzymes belonging to the same family of the α-amylase specifically known as glycosyl-hydrolase family 13. This peculiar enzyme is capable of catalyzing more than one reaction with the most important being the synthesis of non-reducing cyclic dextrins known as cyclodextrins starting from starch, amylose, and other polysaccharides.
Levansucrase is an enzyme that catalyzes the chemical reaction
Hyaluronoglucuronidase is an enzyme with systematic name hyaluronate 3-glycanohydrolase. This enzyme catalyses the following chemical reaction
Lichenase is an enzyme with systematic name (1→3)-(1→4)-β-D-glucan 4-glucanohydrolase. It was named after its activity in on lichenin.
The enzyme exo-(1→4)-α-D-glucan lyase (EC 4.2.2.13, α-(1→4)-glucan 1,5-anhydro-D-fructose eliminase, α-1,4-glucan exo-lyase, α-1,4-glucan lyase, GLase) is an enzyme with systematic name (1→4)-α-D-glucan exo-4-lyase (1,5-anhydro-D-fructose-forming). 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 organisms of the genus Ulva (algae), and some marine bacteria. 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 (11): 3061–5. doi: 10.1016/S0021-9258(20)81309-X . PMID 13762462.
- Meyer K, Rapport MM (1952). "Hyaluronidases". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 13. pp. 199–236. doi:10.1002/9780470122587.ch6. ISBN 978-0-470-64614-4. PMID 14943668.
{{cite book}}:|journal=ignored (help) - 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.
