xanthan lyase | |||||||||
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Identifiers | |||||||||
EC no. | 4.2.2.12 | ||||||||
CAS no. | 113573-69-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme xanthan lyase (EC 4.2.2.12) catalyzes the following process:
It belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Xanthan lyase was first identified and partially purified in 1987. [1]
Xanthan is a polysaccharide secreted by several different bacterial taxa, such as the plant pathogen Xanthomonas campestris , and it consists of a main linear chain based on cellulose with side chains attached to alternate glucosyl (glucose) residues. [2] These side chains contain three monosaccharide residues. Xanthan lyase is produced by bacteria that degrade this polysaccharide, such as Bacillus , Corynebacterium , Bacteroides , Ruminococcaceae , and Paenibacillus species. [2] [3] [4]
Xanthan is used in industry as a thickening agent in foods and drinks, as a stabilizing agent for foams, as a means of enhancing oil recovery and in the manufacture of good such as paints, cosmetics and explosives. [3] The use of xanthan lyase as a means of altering the physical properties of xanthans is an area of current research in biotechnology.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1J0M, 1J0N, 1X1H, 1X1I, 1X1J, 2E22, and 2E24. The enzyme from Bacillus is a monomer consisting of two domains: an alpha helical N-terminal domain, and a C-terminal domain composed of beta sheets. [5] The active site is a deep cleft located between these two domains.
A hemicellulose is one of a number of heteropolymers, such as arabinoxylans, present along with cellulose in almost all terrestrial plant cell walls. Cellulose is crystalline, strong, and resistant to hydrolysis. Hemicelluloses are branched, shorter in length than cellulose, and also show a propensity to crystallize. They can be hydrolyzed by dilute acid or base as well as a myriad of hemicellulase enzymes.
Dictyoglomus is a genus of bacterium, given its own Phylum, called the Dictyoglomi. This organism is extremely thermophilic, meaning it thrives at extremely high temperatures. It is chemoorganotrophic, meaning it derives energy by metabolizing organic molecules. This organism is of interest because it elaborates an enzyme, xylanase, which digests xylan, a heteropolymer of the pentose sugar xylose. By pretreating wood pulp with this enzyme, paper manufacturers can achieve comparable levels of whiteness with much less chlorine bleach.
Polymyxins are antibiotics. Polymyxins B and E are used in the treatment of Gram-negative bacterial infections. They work mostly by breaking up the bacterial cell membrane. They are part of a broader class of molecules called nonribosomal peptides.
In enzymology, a vanillin synthase is an enzyme that catalyzes the chemical reaction
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The enzyme hyaluronate lyase catalyzes the chemical reaction
The enzyme mannuronate-specific alginate lyase catalyzes the degradation of alginate into various monosaccharide and polysaccharide products:
In enzymology, a trans-feruloyl-CoA hydratase (EC 4.2.1.101) is an enzyme that catalyzes the chemical reaction
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In enzymology, a diaminobutyrate-2-oxoglutarate transaminase is an enzyme that catalyzes the chemical reaction
Paenibacillus vortex is a species of pattern-forming bacteria, first discovered in the early 1990s by Eshel Ben-Jacob's group at Tel Aviv University. It is a social microorganism that forms colonies with complex and dynamic architectures. P. vortex is mainly found in heterogeneous and complex environments, such as the rhizosphere, the soil region directly influenced by plant roots.
Paenibacillus dendritiformis is a species of pattern-forming bacteria, first discovered in the early 90s by Eshel Ben-Jacob's group. It is a social microorganism that forms colonies with complex and dynamic architectures. The genus Paenibacillus comprises facultative anaerobic, endospore-forming bacteria originally included within the genus Bacillus and then reclassified as a separate genus in 1993. Bacteria belonging to this genus have been detected in a variety of environments such as: soil, water, rhizosphere, vegetable matter, forage and insect larvae.
In molecular biology, glycoside hydrolase family 88 is a family of glycoside hydrolases.
Glucan 1,4-alpha-maltohydrolase is an enzyme with systematic name 4-alpha-D-glucan alpha-maltohydrolase. 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
Rhamnogalacturonan exolyase is an enzyme with systematic name α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate exolyase. This enzyme catalyses the following chemical reaction
The enzyme Rhamnogalacturonan endolyase is an enzyme with systematic name α-L-rhamnopyranosyl-(1→4)-α-D-galactopyranosyluronate endolyase. catalyses the following process:
Gellan lyase is an enzyme with systematic name gellan β-D-glucopyranosyl-(1→4)-D-glucopyranosyluronate lyase. This enzyme catalyses the following process: