Glycoside Hydrolase Family 18
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Glycoside Hydrolase Family 18
In molecular biology, Glycoside hydrolase family 18 is a family of glycoside hydrolases. Glycoside hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes. Some members of this familyCAZY GH_18 belong to the chitinase class II group which includes chitinase, chitodextrinase and the killer toxin of ''Kluyveromyces lactis''. The chitinases hydrolyse chitin oligosaccharides. Another chitinase II member is the novel gene Chitinase domain-containing protein 1. The family also includes various glycoproteins from mammals; cartilage glycoprotein and the oviduct The oviduct in mammals, is the passageway ...
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Protein Family
A protein family is a group of evolutionarily related proteins. In many cases, a protein family has a corresponding gene family, in which each gene encodes a corresponding protein with a 1:1 relationship. The term "protein family" should not be confused with Family (biology), family as it is used in taxonomy. Proteins in a family descend from a common ancestor and typically have similar protein structure, three-dimensional structures, functions, and significant Sequence homology, sequence similarity. The most important of these is sequence similarity (usually amino-acid sequence), since it is the strictest indicator of homology and therefore the clearest indicator of common ancestry. A fairly well developed framework exists for evaluating the significance of similarity between a group of sequences using sequence alignment methods. Proteins that do not share a common ancestor are very unlikely to show statistically significant sequence similarity, making sequence alignment a powerf ...
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Oligosaccharides
An oligosaccharide (/ˌɑlɪgoʊˈsækəˌɹaɪd/; from the Greek ὀλίγος ''olígos'', "a few", and σάκχαρ ''sácchar'', "sugar") is a saccharide polymer containing a small number (typically two to ten) of monosaccharides (simple sugars). Oligosaccharides can have many functions including cell recognition and cell adhesion. They are normally present as glycans: oligosaccharide chains are linked to lipids or to compatible amino acid side chains in proteins, by ''N''- or ''O''-glycosidic bonds. ''N''-Linked oligosaccharides are always pentasaccharides attached to asparagine via a beta linkage to the amine nitrogen of the side chain.. Alternately, ''O''-linked oligosaccharides are generally attached to threonine or serine on the alcohol group of the side chain. Not all natural oligosaccharides occur as components of glycoproteins or glycolipids. Some, such as the raffinose series, occur as storage or transport carbohydrates in plants. Others, such as maltodextrins or c ...
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Oviduct
The oviduct in mammals, is the passageway from an ovary. In human females this is more usually known as the Fallopian tube or uterine tube. The eggs travel along the oviduct. These eggs will either be fertilized by spermatozoa to become a zygote, or will degenerate in the body. Normally, these are paired structures, but in birds and some cartilaginous fishes, one or the other side fails to develop (together with the corresponding ovary), and only one functional oviduct can be found. Except in teleosts, the oviduct is not directly in contact with the ovary. Instead, the most anterior portion ends in a funnel-shaped structure called the infundibulum, which collects eggs as they are released by the ovary into the body cavity. The only female vertebrates to lack oviducts are the jawless fishes. In these species, the single fused ovary releases eggs directly into the body cavity. The fish eventually extrudes the eggs through a small genital pore towards the rear of the body. Fish and ...
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Cartilage
Cartilage is a resilient and smooth type of connective tissue. In tetrapods, it covers and protects the ends of long bones at the joints as articular cartilage, and is a structural component of many body parts including the rib cage, the neck and the bronchial tubes, and the intervertebral discs. In other taxa, such as chondrichthyans, but also in cyclostomes, it may constitute a much greater proportion of the skeleton. It is not as hard and rigid as bone, but it is much stiffer and much less flexible than muscle. The matrix of cartilage is made up of glycosaminoglycans, proteoglycans, collagen fibers and, sometimes, elastin. Because of its rigidity, cartilage often serves the purpose of holding tubes open in the body. Examples include the rings of the trachea, such as the cricoid cartilage and carina. Cartilage is composed of specialized cells called chondrocytes that produce a large amount of collagenous extracellular matrix, abundant ground substance that is rich in pro ...
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Mammals
Mammals () are a group of vertebrate animals constituting the class Mammalia (), characterized by the presence of mammary glands which in females produce milk for feeding (nursing) their young, a neocortex (a region of the brain), fur or hair, and three middle ear bones. These characteristics distinguish them from reptiles (including birds) from which they diverged in the Carboniferous, over 300 million years ago. Around 6,400 extant species of mammals have been described divided into 29 orders. The largest orders, in terms of number of species, are the rodents, bats, and Eulipotyphla (hedgehogs, moles, shrews, and others). The next three are the Primates (including humans, apes, monkeys, and others), the Artiodactyla ( cetaceans and even-toed ungulates), and the Carnivora (cats, dogs, seals, and others). In terms of cladistics, which reflects evolutionary history, mammals are the only living members of the Synapsida (synapsids); this clade, together with Saur ...
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Glycoproteins
Glycoproteins are proteins which contain oligosaccharide chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling. In contrast, ...
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Chitinase Domain-containing Protein 1
Chitinase domain-containing protein 1 (CHID1) is a highly Conserved sequence, conserved protein of unknown function located on the Chromosome#Metaphase chromatin and division, short (p) arm of chromosome 11 near the telomere. The protein has 27 introns, which allows for many isoforms of this gene. It has several aliases, the most common of which is Stabilin-1 interacting chitinase-like protein (SI-CLP). As indicated by the alias, CHID1 is known to interact with the protein STAB1. CHID1 is expressed ubiquitously at levels nearly 6 times the average gene, and is conserved very far back to organisms such as ''Caenorhabditis elegans'' and possibly some prokaryotes. This protein is known to have Carbohydrate-binding module, carbohydrate binding sites, which could be involved in Carbohydrate catabolism, carbohydrate catabolysis. Gene CHID1 is located on chromosome 11 at the location p15.5. It is just downstream of TSPAN4 and upstream of AP2A2. CHID1 is ubiquitously expressed at a high l ...
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Chitin
Chitin ( C8 H13 O5 N)n ( ) is a long-chain polymer of ''N''-acetylglucosamine, an amide derivative of glucose. Chitin is probably the second most abundant polysaccharide in nature (behind only cellulose); an estimated 1 billion tons of chitin are produced each year in the biosphere. It is a primary component of cell walls in fungi (especially basidiomycetes and filamentous fungi), the exoskeletons of arthropods such as crustaceans and insects, the radulae, cephalopod beaks and gladii of molluscs and in some nematodes and diatoms. It is also synthesised by at least some fish and lissamphibians. Commercially, chitin is extracted from the shells of crabs, shrimps, shellfishes and lobsters, which are major by-products of the seafood industry. The structure of chitin is comparable to cellulose, forming crystalline nanofibrils or whiskers. It is functionally comparable to the protein keratin. Chitin has proved useful for several medicinal, industrial and biotechnological purpos ...
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Glycoside Hydrolase
Glycoside hydrolases (also called glycosidases or glycosyl hydrolases) catalyze the hydrolysis of glycosidic bonds in complex sugars. They are extremely common enzymes with roles in nature including degradation of biomass such as cellulose (cellulase), hemicellulose, and starch (amylase), in anti-bacterial defense strategies (e.g., lysozyme), in pathogenesis mechanisms (e.g., viral neuraminidases) and in normal cellular function (e.g., trimming mannosidases involved in N-linked glycoprotein biosynthesis). Together with glycosyltransferases, glycosidases form the major catalytic machinery for the synthesis and breakage of glycosidic bonds. Occurrence and importance Glycoside hydrolases are found in essentially all domains of life. In prokaryotes, they are found both as intracellular and extracellular enzymes that are largely involved in nutrient acquisition. One of the important occurrences of glycoside hydrolases in bacteria is the enzyme beta-galactosidase (LacZ), which i ...
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Kluyveromyces Lactis
''Kluyveromyces lactis'' is a ''Kluyveromyces'' yeast commonly used for genetic studies and industrial applications. Its name comes from the ability to assimilate lactose and convert it into lactic acid. ''Kluyveromyces lactis'' (formerly ''Saccharomyces lactis'') is a yeast which has the ability to assimilate lactose and convert it into lactic acid. ''K. lactis'' and other organisms i.e., ''Aspergillus niger'' var awamori and ''Escherichia coli'' K-12 are grown in fermenters to produce chymosin ( rennet) on a commercial scale; this rennet, which replaces the conventional form obtained from slaughtered animals, is now widely used in cheese production. Yeasts and fungi are ideal organisms for comparative genomic studies in eukaryotes because of their small and compact genomes and because they include a number of species such as ''Neurospora crassa'', ''Saccharomyces cerevisiae'' and ''Schizosaccharomyces pombe'', that have been, and continue to be, used extensively in genetic st ...
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Chitinase
Chitinases (EC 3.2.1.14, chitodextrinase, 1,4-β-poly-N-acetylglucosaminidase, poly-β-glucosaminidase, β-1,4-poly-N-acetyl glucosamidinase, poly ,4-(N-acetyl-β-D-glucosaminide)glycanohydrolase, (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase; systematic name (1→4)-2-acetamido-2-deoxy-β-D-glucan glycanohydrolase) are hydrolytic enzymes that break down glycosidic bonds in chitin. They catalyse the following reaction: : Random endo-hydrolysis of ''N''-acetyl-β-D-glucosaminide (1→4)-β-linkages in chitin and chitodextrins As chitin is a component of the cell walls of fungi and exoskeletal elements of some animals (including mollusks and arthropods), chitinases are generally found in organisms that either need to reshape their own chitin or dissolve and digest the chitin of fungi or animals. Species distribution Chitinivorous organisms include many bacteria ( Aeromonads, ''Bacillus'', ''Vibrio'', among others), which may be pathogenic or detritivorous. The ...
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