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Both domains are located at the N-terminal portion of the protein which is not the case for most other double C2 domain proteins, and their role is most similar to that carried out by proteins that exhibit a single C2 domain. The core domain located at the C-terminus part of the copine is found to have a unique and conserved primary sequence. The function of the core domain is still uncertain, however, researchers believe it has a similar function to the "A domain" in integrins. This similarity in function involves serving as a binding site for target proteins, and is supported by evidence that the copine core domain exhibits secondary and tertiary structures comparable to the integrin A domain. == References == | https://en.wikipedia.org/wiki/Copine |
In molecular biology, ecotin is a protease inhibitor which belongs to MEROPS inhibitor family I11, clan IN. Ecotins are dimeric periplasmic proteins from Escherichia coli and related Gram-negative bacteria that have been shown to be potent inhibitors of many trypsin-fold serine proteases of widely varying substrate specificity, which belong to MEROPS peptidase family S1. Phylogenetic analysis suggested that ecotin has an exogenous target, possibly neutrophil elastase. Ecotin from E. coli, Yersinia pestis, and Pseudomonas aeruginosa, all species that encounter the mammalian immune system, inhibit neutrophil elastase strongly while ecotin from the plant pathogen Pantoea citrea inhibits neutrophil elastase 1000-fold less potently. Ecotins all potently inhibit pancreatic digestive peptidases trypsin and chymotrypsin, while showing more variable inhibition of the blood peptidases Factor Xa, thrombin, and urokinase-type plasminogen activator. | https://en.wikipedia.org/wiki/Ecotin |
In molecular biology, elicitins are a family of small, highly conserved proteins secreted by phytopathogenic microorganisms belonging to the Phytophthora and Pythium species. They are toxic proteins responsible for inducing a necrotic and systemic hypersensitive response in plants from the Solanaceae and Cruciferae families. Leaf necrosis provides immediate control of fungal invasion and induces systemic acquired resistance; both responses mediate basic protection against subsequent pathogen inoculation. Members of this family share a high level of sequence similarity, but they differ in net charge, dividing them into two classes: alpha and beta. | https://en.wikipedia.org/wiki/Elicitin |
Alpha-elicitins are highly acidic, with a valine residue at position 13, whereas beta-elicitins are basic, with a lysine at the same position. Residue 13 is known to be involved in the control of necrosis and, being exposed, is thought to be involved in ligand/receptor binding. Phenotypically, the two classes can be distinguished by their necrotic properties: beta-elicitins are 100-fold more toxic and provide better subsequent protection. == References == | https://en.wikipedia.org/wiki/Elicitin |
In molecular biology, entericidins are bacterial antidote/toxin peptides. The entericidin locus is activated in the stationary phase of growth under high osmolarity conditions by rho-S and simultaneously repressed by the osmoregulatory EnvZ/OmpR signal transduction pathway. The entericidin locus encodes tandem paralogous genes (ecnAB) and directs the synthesis of two small cell-envelope lipoproteins (entericidin A and entericidin B) which can maintain plasmids in bacterial population by means of post-segregational killing. == References == | https://en.wikipedia.org/wiki/Entericidin |
In molecular biology, enzymes containing the cyclodeaminase domain function in channeling one-carbon units to the folate pool. In most cases, this domain acts as a formimidoyltetrahydrofolate cyclodeaminase, which catalyses the cyclisation of formimidoyltetrahydrofolate to methenyltetrahydrofolate as shown in reaction (1). In the methylotrophic bacterium Methylobacterium extorquens, however, it acts as a methenyltetrahydrofolate cyclohydrolase, which catalyses the interconversion of formyltetrahydrofolate and methylenetetrahydrofolate, as shown in reaction (2). (1) 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH(3) (2) 10- formyltetrahydrofolate = 5,10-methenyltetrahydrofolate + H(2)O In prokaryotes, this domain mostly occurs on its own, while in eukaryotes it is fused to a glutamate formiminotransferase domain (which catalyses the previous step in the pathway) to form the bifunctional enzyme formiminotransferase cyclodeaminase. | https://en.wikipedia.org/wiki/Cyclodeaminase_domain |
The eukaryotic enzyme is a circular tetramer of homodimers, while the prokaryotic enzyme is a dimer.The crystal structure of the cyclodeaminase enzyme from Thermaotogoa maritima has been studied. It is a homodimer, where each monomer is composed of six alpha helices arranged in an up and down helical bundle, forming a novel fold. | https://en.wikipedia.org/wiki/Cyclodeaminase_domain |
The location of the active site is not known, but sequence alignments revealed two clusters of conserved residues located in a deep pocket within the dimmer interface. This pocket was large enough to accommodate the reaction product and it was postulated that this is the active site. == References == | https://en.wikipedia.org/wiki/Cyclodeaminase_domain |
In molecular biology, enzymes in the DNA/RNA non-specific endonuclease family of bacterial and eukaryotic endonucleases EC 3.1.30.- share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity. A histidine has been shown to be essential for the activity of the Serratia marcescens nuclease. This residue is located in a conserved region which also contains an aspartic acid residue that could be implicated in the binding of the divalent ion.Notable members of the family include Serratia marcescens NucA and human Exonuclease G. == References == | https://en.wikipedia.org/wiki/DNA/RNA_non-specific_endonuclease |
In molecular biology, excisionase is a bacteriophage protein encoded by the Xis gene. It is involved in excisive recombination by regulating the assembly of the excisive intasome and by inhibiting viral integration. It adopts an unusual winged-helix structure in which two alpha helices are packed against two extended strands. Also present in the structure is a two-stranded anti-parallel beta-sheet, whose strands are connected by a four-residue wing. | https://en.wikipedia.org/wiki/Excisionase |
During interaction with DNA, helix alpha2 is thought to insert into the major groove, while the wing contacts the adjacent minor groove or phosphodiester backbone. The C-terminal region of excisionase is involved in interaction with phage-encoded integrase (Int), and a putative C-terminal alpha helix may fold upon interaction with Int and/or DNA. == References == | https://en.wikipedia.org/wiki/Excisionase |
In molecular biology, exon skipping is a form of RNA splicing used to cause cells to “skip” over faulty or misaligned sections (exons) of genetic code, leading to a truncated but still functional protein despite the genetic mutation. | https://en.wikipedia.org/wiki/Exon_skipping |
In molecular biology, extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinase intracellular signalling molecules that are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells. Many different stimuli, including growth factors, cytokines, virus infection, ligands for heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.The term, "extracellular signal-regulated kinases", is sometimes used as a synonym for mitogen-activated protein kinase (MAPK), but has more recently been adopted for a specific subset of the mammalian MAPK family.In the MAPK/ERK pathway, Ras activates c-Raf, followed by mitogen-activated protein kinase kinase (abbreviated as MKK, MEK, or MAP2K) and then MAPK1/2 (below). Ras is typically activated by growth hormones through receptor tyrosine kinases and GRB2/SOS, but may also receive other signals. ERKs are known to activate many transcription factors, such as ELK1, and some downstream protein kinases. Disruption of the ERK pathway is common in cancers, especially Ras, c-Raf, and receptors such as HER2. | https://en.wikipedia.org/wiki/Extracellular_signal-regulated_kinase |
In molecular biology, fibrous proteins or scleroproteins are one of the three main classifications of protein structure (alongside globular and membrane proteins). Fibrous proteins are made up of elongated or fibrous polypeptide chains which form filamentous and sheet-like structures. These kind of protein can be distinguished from globular protein by its low solubility in water. | https://en.wikipedia.org/wiki/Fibrous_protein |
Such proteins serve protective and structural roles by forming connective tissue, tendons, bone matrices, and muscle fiber. Fibrous proteins consist of many superfamilies including keratin, collagen, elastin, and fibrin. Collagen is the most abundant of these proteins which exists in vertebrate connective tissue including tendon, cartilage, and bone. | https://en.wikipedia.org/wiki/Fibrous_protein |
In molecular biology, foldases are a particular kind of molecular chaperones that assist the non-covalent folding of proteins in an ATP-dependent manner. Examples of foldase systems are the GroEL/GroES and the DnaK/DnaJ/GrpE system. | https://en.wikipedia.org/wiki/Foldase |
In molecular biology, for Homo sapiens snoRA35 (also known as HBI-36) is an H/ACA box snoRNA, first cloned from a mouse adult brain cDNA library by Cavaillé et al. (2000), and found to be specifically expressed in the choroid plexus. Its human orthologue, HBI-36 was discovered by a homology search, and was found to be specifically expressed in the brain. Its gene resides in the second intron of the serotonin receptor 2c (5HT-2c) gene, which is predominantly expressed in choroid plexus epithelial cells. The human 5HT-2c mRNA was predicted to be 2'O-methylated by the C/D box snoRNP HBII-52 at a position also subjected to A:I editing. HBI-36 has no documented RNA target. | https://en.wikipedia.org/wiki/Small_nucleolar_RNA_SNORA35 |
In molecular biology, gel extraction or gel isolation is a technique used to isolate a desired fragment of intact DNA from an agarose gel following agarose gel electrophoresis. After extraction, fragments of interest can be mixed, precipitated, and enzymatically ligated together in several simple steps. This process, usually performed on plasmids, is the basis for rudimentary genetic engineering. After DNA samples are run on an agarose gel, extraction involves four basic steps: identifying the fragments of interest, isolating the corresponding bands, isolating the DNA from those bands, and removing the accompanying salts and stain. | https://en.wikipedia.org/wiki/Gel_extraction |
To begin, UV light is shone on the gel in order to illuminate all the ethidium bromide-stained DNA. Care must be taken to avoid exposing the DNA to mutagenic radiation for longer than absolutely necessary. The desired band is identified and physically removed with a cover slip or razor blade. The removed slice of gel should contain the desired DNA inside. An alternative method, utilizing SYBR Safe DNA gel stain and blue-light illumination, avoids the DNA damage associated with ethidium bromide and UV light.Several strategies for isolating and cleaning the DNA fragment of interest exist. | https://en.wikipedia.org/wiki/Gel_extraction |
In molecular biology, genome architecture mapping (GAM) is a cryosectioning method to map colocalized DNA regions in a ligation independent manner. It overcomes some limitations of Chromosome conformation capture (3C), as these methods have a reliance on digestion and ligation to capture interacting DNA segments. GAM is the first genome-wide method for capturing three-dimensional proximities between any number of genomic loci without ligation.The sections that are found using the cryosectioning method mentioned above are referred to as nuclear profiles. | https://en.wikipedia.org/wiki/Nuclear_profile |
The information that they provide relates to their coverage across a genome. A large set of values can be produced that represents the strength of nuclear profiles’ presence within a genome. Based on how large or small the coverage across a genome is, judgements can be made involving chromatin interactions, nuclear profile location within the nucleus being cryosectioned, and chromatin compaction levels.To be able to visualize this information, certain methods can be implemented using the raw data given by a table that shows whether or not nuclear profiles are detected in a genomic window, the genomic windows being represented within a certain chromosome. | https://en.wikipedia.org/wiki/Nuclear_profile |
With a 1 representing a detection within a window and a 0 representing no detection, subsets of data can be obtained and interpreted by creating graphs, charts, heatmaps, and other visualization methods that allow these subsets to be seen in ways other than binary detection methods. By using a more graphic approach to interpreting the data obtained with cryosectioning, it is possible to see interactions that would have otherwise not been seen before. Some examples of how these visuals can be interpreted include bar graphs that show the radial position and chromatin compaction levels of nuclear profiles, they can be split into categories to give a generalization of how often nuclear profiles are detected within a genomic window. | https://en.wikipedia.org/wiki/Nuclear_profile |
A radar chart is a circular graph that represents the percentages of occurrence within a number of variables. In the sense of genomic information, radar charts can be used to show how genomic windows are represented within “features” of the genome that are part of certain regions that make it up. These charts can be made to compare groups of nuclear profiles with each other and their differences in how they occur within these features is shown graphically. | https://en.wikipedia.org/wiki/Nuclear_profile |
Heatmaps are another form of visual representation where individual values in a table are shown by cells that take on different colors based on their value. This allows for trends to be seen within a table by the display of groups of similar colors or the lack of. The heatmap to the right represents the relationship between nuclear profiles based on a calculated Jaccard Index where the values ranging from 0-1 are the degree of similarity between two nuclear profiles. | https://en.wikipedia.org/wiki/Nuclear_profile |
Showing this similarity can help to display where certain groups of nuclear profiles are more common within a genome. In this heatmap the diagonal white line of cells is expected because these cells indicate where nuclear profiles intersect themselves and are therefore the most similar as possible to each other, which gives them a value of 1. In addition to the white diagonal line of cells, a cluster of other lightly colored cells can be observed in the bottom right of the heatmap. | https://en.wikipedia.org/wiki/Nuclear_profile |
This grouping of nuclear profiles display high similarity using the Jaccard Index. This means that the nuclear profiles are present in a greater number of genomic windows than others. The bar graph to the right represents the percentage of nuclear profiles that belong to a category of radial position (with 5 being strongly equatorial and 1 being strongly apical). | https://en.wikipedia.org/wiki/Nuclear_profile |
The cluster of nuclear profiles was calculated based on their similarity to each other using a k-means clustering method. To begin the process, three nuclear profiles were chosen at random as the ‘centers’ of the cluster. After the centers were chosen at random, every other nuclear profile is assigned to a cluster based on its distance from each center using a calculated distance value. | https://en.wikipedia.org/wiki/Nuclear_profile |
New centers were then chosen to better represent the cluster. This process was repeated until the centers at the start matched the centers at the end. When the cluster centers have not changed, it could be interpreted that this means proper clusters have been chosen. | https://en.wikipedia.org/wiki/Nuclear_profile |
Within each of these clusters the nuclear profiles are then given a value from 1 to 5 based on their radial position and this data is fed into a bar graph to give a visualization. This radar chart to the right shows 3 clusters of nuclear profiles’ percentage of occurrence within certain features of the mouse genome. Each cluster of nuclear profiles was calculated using the k-means clustering technique described above, relating to the bar graph showing radial positions of nuclear profiles. | https://en.wikipedia.org/wiki/Nuclear_profile |
Comparisons can be made between the clusters and how they show up more or less in certain features in contrast to each other. To calculate a cluster's presence within a certain feature, it is determined if a nuclear profile is present within a window that is detected within a feature. The percentage of how often nuclear profiles within a cluster occur within the same windows that are detected within a feature are then displayed by the radar chart. | https://en.wikipedia.org/wiki/Nuclear_profile |
In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p-aminobenzoate, and glutamine-dependent carbamoyl-transferase (CPSase). Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence similarities two classes of GATase domains have been identified: class-I (also known as trpG-type) and class-II (also known as purF-type). | https://en.wikipedia.org/wiki/Glutamine_amidotransferase |
Class-I GATase domains are defined by a conserved catalytic triad consisting of cysteine, histidine and glutamate. Class-I GATase domains have been found in the following enzymes: the second component of anthranilate synthase and 4-amino-4-deoxychorismate (ADC) synthase; CTP synthase; GMP synthase; glutamine-dependent carbamoyl-phosphate synthase; phosphoribosylformylglycinamidine synthase II; and the histidine amidotransferase hisH. == References == | https://en.wikipedia.org/wiki/Glutamine_amidotransferase |
In molecular biology, glycoside hydrolase family 100 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 100 CAZY GH_100 includes enzymes with invertase activity EC 3.2.1.26. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_100 |
In molecular biology, glycoside hydrolase family 101 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family GH101 includes enzymes with endo-α-N-acetylgalactosaminidase EC 3.2.1.97 activity and can be split into several subfamilies. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_101 |
In molecular biology, glycoside hydrolase family 108 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 108 CAZY GH_108 includes enzymes with lysozyme (N-acetylmuramidase) EC 3.2.1.17 activity. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_108 |
A glutamic acid residue within a conserved Glu-Gly-Gly-Tyr motif is essential for catalytic activity. In bacteria, it may activate the secretion of large proteins via the breaking and rearrangement of the peptidoglycan layer during secretion. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_108 |
In molecular biology, glycoside hydrolase family 13 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Enzymes containing this domain belong to family 13 (CAZY GH_13) of the glycosyl hydrolases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_13 |
The maltogenic alpha-amylase is an enzyme which catalyses hydrolysis of (1-4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha-maltose residues from the non-reducing ends of the chains in the conversion of starch to maltose. Other enzymes in this family include neopullulanase, which hydrolyses pullulan to panose, and cyclomaltodextrinase, which hydrolyses cyclodextrins. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_13 |
In molecular biology, glycoside hydrolase family 15 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_15 |
y9 Glycoside hydrolase family 15 CAZY GH_15 comprises enzymes with several known activities; glucoamylase (EC 3.2.1.3); alpha-glucosidase (EC 3.2.1.20); glucodextranase (EC 3.2.1.70). Glucoamylase (GA) catalyses the release of D-glucose from the non-reducing ends of starch and other oligo- or poly-saccharides. Studies of fungal GA have indicated 3 closely clustered acidic residues that play a role in the catalytic mechanism. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_15 |
This region is also conserved in a recently sequenced bacterial GA.The 3D structure of the pseudo-tetrasaccharide acarbose complexed with glucoamylase II(471) from Aspergillus awamori var. X100 has been determined to 2.4A resolution. The protein belongs to the mainly alpha class, and contains 19 helices and 9 strands. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_15 |
In molecular biology, glycoside hydrolase family 20 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 20 CAZY GH_20 comprises enzymes with several known activities; beta-hexosaminidase (EC 3.2.1.52); lacto-N-biosidase (EC 3.2.1.140). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_20 |
Carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base in this family of enzymes. In the brain and other tissues, beta-hexosaminidase A degrades GM2 gangliosides; specifically, the enzyme hydrolyses terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer, with one alpha, one beta-A and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; and hexosaminidase S is a homodimer of alpha chains. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_20 |
The two beta chains are derived from the cleavage of a precursor. Mutations in the beta-chain lead to Sandhoff disease, a lysosomal storage disorder characterised by accumulation of GM2 ganglioside. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_20 |
In molecular biology, glycoside hydrolase family 22 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 22 CAZY GH_22 comprises lysozyme type C (EC 3.2.1.17) lysozyme type i (EC 3.2.1.17) and alpha-lactalbumins. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_22 |
Asp and/or the carbonyl oxygen of the C-2 acetamido group of the substrate acts as the catalytic nucleophile/base. Alpha-lactalbumin, is a milk protein that acts as the regulatory subunit of lactose synthetase, acting to promote the conversion of galactosyltransferase to lactose synthase, which is essential for milk production. In the mammary gland, alpha-lactalbumin changes the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_22 |
Lysozymes act as bacteriolytic enzymes by hydrolyzing the beta(1->4) bonds between N-acetylglucosamine and N-acetylmuramic acid in the peptidoglycan of prokaryotic cell walls. It has also been recruited for a digestive role in certain ruminants and colobine monkeys. There are at least five different classes of lysozymes: C (chicken type), G (goose type), phage-type (T4), fungi (Chalaropsis), and bacterial (Bacillus subtilis). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_22 |
There are few similarities in the sequences of the different types of lysozymes. Lysozyme type C and alpha-lactalbumin are similar both in terms of primary sequence and structure, and probably evolved from a common ancestral protein. Around 35 to 40% of the residues are conserved in both proteins as well as the positions of the four disulphide bonds. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_22 |
There is, however, no similarity in function. Another significant difference between the two enzymes is that all lactalbumins have the ability to bind calcium, while this property is restricted to only a few lysozymes.The binding site was deduced using high resolution X-ray structure analysis and was shown to consist of three aspartic acid residues. It was first suggested that calcium bound to lactalbumin stabilised the structure, but recently it has been claimed that calcium controls the release of lactalbumin from the golgi membrane and that the pattern of ion binding may also affect the catalytic properties of the lactose synthetase complex. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_22 |
In molecular biology, glycoside hydrolase family 24 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 24 CAZY GH_24 comprises enzymes with only one known activity; lysozyme (EC 3.2.1.17). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_24 |
This family includes lambda phage lysozyme and Escherichia coli T4 phage endolysin. Lysozyme helps to release mature phage particles from the cell wall by breaking down the peptidoglycan. The enzyme hydrolyses the 1,4-beta linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of prokaryotic cell walls. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_24 |
E. coli endolysin also functions in bacterial cell lysis and acts as a transglycosylase. The T4 lysozyme structure contains 2 domains, the interface between which forms the active-site cleft. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_24 |
The N-terminus of the 2 domains undergoes a 'hinge-bending' motion about an axis passing through the molecular waist. This mobility is thought to be important in allowing access of substrates to the enzyme active site. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_24 |
In molecular biology, glycoside hydrolase family 25 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 25 CAZY GH_25 comprises enzymes with only one known activity; lysozyme (EC 3.2.1.17). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_25 |
It has been shown that a number of cell-wall lytic enzymes are evolutionary related and can be classified into a single family. Two residues, an aspartate and a glutamate, have been shown to be important for the catalytic activity of the Charalopsis enzyme. These residues as well as some others in their vicinity are conserved in all proteins from this family. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_25 |
In molecular biology, glycoside hydrolase family 26 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 26 CAZY GH_26 comprises enzymes with two known activities; mannanase (EC 3.2.1.78) and β-1,3-xylanase (EC 3.2.1.32). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_26 |
Family 26 encompasses mainly mannan endo-1,4-beta-mannosidases. Mannan endo-1,4-beta-mannosidase hydrolyses mannan and galactomannan, but displays little activity towards other plant cell wall polysaccharides. The enzyme randomly hydrolyses 1,4-beta-D-linkages in mannans, galacto-mannans, glucomannans and galactoglucomannans. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_26 |
In molecular biology, glycoside hydrolase family 27 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_27 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 27 together with family 31 and the family 36 alpha-galactosidases form the glycosyl hydrolase clan GH-D, a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a common catalytic mechanism and structural topology. Alpha-galactosidase (EC 3.2.1.22) (melibiase) catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_27 |
Alpha-galactosidase is present in a variety of organisms. There is a considerable degree of similarity in the sequence of alpha-galactosidase from various eukaryotic species. Escherichia coli alpha-galactosidase (gene melA), which requires NAD and magnesium as cofactors, is not structurally related to the eukaryotic enzymes; by contrast, an Escherichia coli plasmid encoded alpha-galactosidase (gene rafA P16551) contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_27 |
Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D- galactosaminides. In man, the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases. The sequence of this enzyme is highly related to that of the eukaryotic alpha-galactosidases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_27 |
In molecular biology, glycoside hydrolase family 28 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 28 CAZY GH_28 comprises enzymes with several known activities; polygalacturonase (EC 3.2.1.15); exo-polygalacturonase (EC 3.2.1.67); exo-polygalacturonase (EC 3.2.1.82); rhamnogalacturonase (EC not defined). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_28 |
Polygalacturonase (PG) (pectinase) catalyzes the random hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans. In fruit, polygalacturonase plays an important role in cell wall metabolism during ripening. In plant bacterial pathogens such as Erwinia carotovora or Ralstonia solanacearum (Pseudomonas solanacearum) and fungal pathogens such as Aspergillus niger, polygalacturonase is involved in maceration and soft-rotting of plant tissue. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_28 |
Exo-poly-alpha-D-galacturonosidase (EC 3.2.1.82) (exoPG) hydrolyzes peptic acid from the non-reducing end, releasing digalacturonate. PG and exoPG share a few regions of sequence similarity, and belong to family 28 of the glycosyl hydrolases. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_28 |
In molecular biology, glycoside hydrolase family 29 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 29 includes alpha-L-fucosidases, They are lysosomal enzymes responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_29 |
Alpha-L-fucosidase is responsible for hydrolysing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Fucosylated glycoconjugates are involved in numerous biological events, making alpha-l-fucosidases, the enzymes responsible for their processing, critically important. Deficiency in alpha-l-fucosidase activity is associated with fucosidosis, a lysosomal storage disorder characterised by rapid neurodegeneration, resulting in severe mental and motor deterioration. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_29 |
The enzyme is a hexamer and displays a two-domain fold, composed of a catalytic (beta/alpha)(8)-like domain and a C-terminal beta-sandwich domain.Drosophila melanogaster spermatozoa contains an alpha-l-fucosidase that might be involved in fertilisation by interacting with alpha-l-fucose residues on the micropyle of the eggshell. In human sperm, membrane-associated alpha-l-fucosidase is stable for extended periods of time, which is made possible by membrane domains and compartmentalisation. These help preserve protein integrity. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_29 |
In molecular biology, glycoside hydrolase family 3 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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 over 100 different families. This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 3 CAZY GH_3 comprises enzymes with a number of known activities; beta-glucosidase (EC 3.2.1.21); beta-xylosidase (EC 3.2.1.37); N-acetyl beta-glucosaminidase (EC 3.2.1.52); glucan beta-1,3-glucosidase (EC 3.2.1.58); cellodextrinase (EC 3.2.1.74); exo-1,3-1,4-glucanase (EC 3.2.1). These enzymes are two-domain globular proteins that are N-glycosylated at three sites. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_3 |
In molecular biology, glycoside hydrolase family 30 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 30 CAZY GH_30 includes the mammalian glucosylceramidases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_30 |
Human acid beta-glucosidase (D-glucosyl-N-acylsphingosine glucohydrolase), cleaves the glucosidic bonds of glucosylceramide and synthetic beta-glucosides. Any one of over 50 different mutations in the gene of glucocerebrosidase have been found to affect activity of this hydrolase, producing variants of Gaucher disease, the most prevalent lysosomal storage disease. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_30 |
In molecular biology, glycoside hydrolase family 31 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 31 CAZY GH_31 comprises enzymes with several known activities; alpha-glucosidase (EC 3.2.1.20), alpha-galactosidase (EC 3.2.1.22); glucoamylase (EC 3.2.1.3), sucrase-isomaltase (EC 3.2.1.48) (EC 3.2.1.10); alpha-xylosidase (EC 3.2.1); alpha-glucan lyase (EC 4.2.2.13). Glycoside hydrolase family 31 groups a number of glycosyl hydrolases on the basis of sequence similarities An aspartic acid has been implicated in the catalytic activity of sucrase, isomaltase, and lysosomal alpha-glucosidase. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_31 |
In molecular biology, glycoside hydrolase family 32 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_32 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Family 32 glycosyl hydrolases comprise two distinct domains. The N-terminal domain, which forms a five bladed beta propeller, and the C-terminal domain, which forms a beta sandwich structure. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_32 |
In molecular biology, glycoside hydrolase family 33 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.This family contains sialidases (CAZY GH_33), which hydrolyse alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)-glycosidic linkages of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_33 |
Sialidases may act as pathogenic factors in microbial infections. The 1.8 A structure of trans-sialidase from leech (Macrobdella decora, Q27701) in complex with 2-deoxy-2, 3-didehydro-NeuAc was solved. The refined model comprising residues 81-769 has a catalytic beta-propeller domain, a N-terminal lectin-like domain and an irregular beta-stranded domain inserted into the catalytic domain. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_33 |
In molecular biology, glycoside hydrolase family 35 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_35 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 35 CAZY GH_35 comprises enzymes with only one known activity; beta-galactosidase (EC 3.2.1.23). Mammalian beta-galactosidase is a lysosomal enzyme (gene GLB1) which cleaves the terminal galactose from gangliosides, glycoproteins, and glycosaminoglycans and whose deficiency is the cause of the genetic disease Gm(1) gangliosidosis (Morquio disease type B). == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_35 |
In molecular biology, glycoside hydrolase family 36 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_36 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 36 together with family 31 and family 27 alpha-galactosidases form the glycosyl hydrolase clan GH-D, a superfamily of alpha-galactosidases, alpha-N-acetylgalactosaminidases, and isomaltodextranases which are likely to share a common catalytic mechanism and structural topology. Alpha-galactosidase (EC 3.2.1.22) (melibiase) catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_36 |
Alpha-galactosidase is present in a variety of organisms. There is a considerable degree of similarity in the sequence of alpha-galactosidase from various eukaryotic species. Escherichia coli alpha-galactosidase (gene melA), which requires NAD and magnesium as cofactors, is not structurally related to the eukaryotic enzymes; by contrast, an Escherichia coli plasmid encoded alpha-galactosidase (gene rafA P16551) contains a region of about 50 amino acids which is similar to a domain of the eukaryotic alpha-galactosidases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_36 |
Alpha-N-acetylgalactosaminidase (EC 3.2.1.49) catalyzes the hydrolysis of terminal non-reducing N-acetyl-D-galactosamine residues in N-acetyl-alpha-D- galactosaminides. In man, the deficiency of this enzyme is the cause of Schindler and Kanzaki diseases. The sequence of this enzyme is highly related to that of the eukaryotic alpha-galactosidases. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_36 |
This family also includes raffinose synthase proteins, also known as seed inhibition (Sip1) proteins. Raffinose (O-alpha- D-galactopyranosyl- (1-->6)- O-alpha- D-glucopyranosyl-(1<-->2)- O-beta- D-fructofuranoside) is a widespread oligosaccharide in plant seeds and other tissues. Raffinose synthase EC 2.4.1.82 is the key enzyme that channels sucrose into the raffinose oligosaccharide pathway.Glycoside hydrolase family 36 also includes enzymes with α-N-acetylgalactosaminidase EC 3.2.1.49 and stachyose synthase EC 2.4.1.67 activities. Glycoside hydrolase family 36 can be subdivided into 11 families, GH36A to GH36K. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_36 |
In molecular biology, glycoside hydrolase family 37 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 37 CAZY GH_37 comprises enzymes with only one known activity; trehalase (EC 3.2.1.28). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_37 |
Trehalase is the enzyme responsible for the degradation of the disaccharide alpha,alpha-trehalose yielding two glucose subunits. It is an enzyme found in a wide variety of organisms and whose sequence has been highly conserved throughout evolution. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_37 |
In molecular biology, glycoside hydrolase family 38 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 38 CAZY GH_38 comprises enzymes with only one known activity; alpha-mannosidase (EC 3.2.1.24) (EC 3.2.1.114). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_38 |
Lysosomal alpha-mannosidase is necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. The enzyme catalyzes the hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides, and can cleave all known types of alpha-mannosidic linkages. Defects in the gene cause lysosomal alpha-mannosidosis (AM), a lysosomal storage disease characterised by the accumulation of unbranched oligo-saccharide chains. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_38 |
A domain, which is found in the central region adopts a structure consisting of three alpha helices, in an immunoglobulin/albumin-binding domain-like fold. The domain is predominantly found in the enzyme alpha-mannosidase. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_38 |
In molecular biology, glycoside hydrolase family 39 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 39 CAZY GH_39 comprises enzymes with several known activities; alpha-L-iduronidase (EC 3.2.1.76); beta-xylosidase (EC 3.2.1.37). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_39 |
The most highly conserved regions in these enzymes are located in their N-terminal sections. These contain a glutamic acid residue which, on the basis of similarities with other families of glycosyl hydrolases, probably acts as the proton donor in their catalytic mechanism. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_39 |
In molecular biology, glycoside hydrolase family 4 is a family of glycoside hydrolases EC 3.2.1., which 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.Glycoside hydrolase family 4 CAZY GH_4 comprises enzymes with several known activities; 6-phospho-beta-glucosidase (EC 3.2.1.86); 6-phospho-alpha-glucosidase (EC 3.2.1.122); alpha-galactosidase (EC 3.2.1.22); alpha-D-glucuronidase (EC 3.2.1.139). 6-phospho-alpha-glucosidase requires both NAD(H) and divalent metal (Mn2+, Fe2+, Co2+, or Ni2+) for activity. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_4 |
In molecular biology, glycoside hydrolase family 42 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.The glycosyl hydrolase 42 family CAZY GH_42 comprises beta-galactosidase enzymes (EC 3.2.1.23). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_42 |
These enzyme catalyse the hydrolysis of terminal, non-reducing terminal beta-D-galactoside residues. The middle domain of these three-domain enzymes is involved in trimerisation. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_42 |
In molecular biology, glycoside hydrolase family 43 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 43 CAZY GH_43 includes enzymes with the following activities, beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55); arabinanase (EC 3.2.1.99), and xylanase (EC 3.2.1.8). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_43 |
The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_43 |
In molecular biology, glycoside hydrolase family 44 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_44 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 44 CAZY GH_44, formerly known as cellulase family J, includes enzymes with endoglucanase EC 3.2.1.4 and xyloglucanase EC 3.2.1.151 activities. The overall structure of enzymes in this family consists of a TIM-like barrel domain, a beta-sandwich domain and an active site with two glutamic acid residues, all of which are conserved between the endoglucanases and xyloglucanases in the family, with only minor differences. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_44 |
In molecular biology, glycoside hydrolase family 45 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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.Glycoside hydrolase family 45 CAZY GH_45 comprises enzymes with only one known activity; endoglucanase (EC 3.2.1.4). | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_45 |
This family is also known as cellulase family K. The best conserved region in these enzymes is located in the N-terminal section. It contains an aspartic acid residue which has been shown to act as a nucleophile in the catalytic mechanism. This also has several cysteines that are involved in forming disulphide bridges. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_45 |
In molecular biology, glycoside hydrolase family 46 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. 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. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_46 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 46 CAZY GH_46 comprises enzymes with only one known activity; chitosanase (EC 3.2.1.132). Chitosanase enzymes catalyse the endohydrolysis of beta-1,4-linkages between N-acetyl-D-glucosamine and D-glucosamine residues in a partly acetylated chitosan. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_46 |
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