id stringlengths 14 14 | text stringlengths 9 3.55k | source stringlengths 1 250 |
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c_ptsw31c86w5l | 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 con... | Copine |
c_4khw6sychtw2 | 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 spe... | Ecotin |
c_t6k5szjs81zl | 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 fam... | Elicitin |
c_bkgs61hlusej | 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 di... | Elicitin |
c_tqr2eqg7krjc | 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 paralogo... | Entericidin |
c_8ffws6wgvlna | 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 ... | Cyclodeaminase domain |
c_d8x052nh5zdn | 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 ... | Cyclodeaminase domain |
c_z328ueoekip4 | 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 == | Cyclodeaminase domain |
c_5ugzec8wwz9j | 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.... | DNA/RNA non-specific endonuclease |
c_7rhg9wlu1rwr | 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 s... | Excisionase |
c_xx4lqf7uv9dh | 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 inte... | Excisionase |
c_vtn6hh1qmt4r | 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. | Exon skipping |
c_d85dzg1zh26n | 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, incl... | Extracellular signal-regulated kinase |
c_dzdjqw9l2qtc | 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 disti... | Fibrous protein |
c_4ziy8cje43u6 | 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 includ... | Fibrous protein |
c_8z8t8twps2lh | 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. | Foldase |
c_7nea80fjs3pq | 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 ... | Small nucleolar RNA SNORA35 |
c_nz0siy9o3bef | 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, u... | Gel extraction |
c_9e4ugn9yjqv2 | 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 s... | Gel extraction |
c_rualhb0jasuk | 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 i... | Nuclear profile |
c_vku6nyciho9y | 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 pro... | Nuclear profile |
c_whn5g3j8u4qa | 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 ... | Nuclear profile |
c_ygha4ghrwijv | 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 ma... | Nuclear profile |
c_xyx7p6156es3 | 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 be... | Nuclear profile |
c_g3dy7do6xgnj | 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 ... | Nuclear profile |
c_21fg7psed3o4 | 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 stro... | Nuclear profile |
c_iqlpe5aiqous | 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 base... | Nuclear profile |
c_3gr0fu8hz9uk | 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. | Nuclear profile |
c_eju0h53ixua8 | 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. Ea... | Nuclear profile |
c_56qlloqu85ap | 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 nuclea... | Nuclear profile |
c_cmk0f4uf8ogs | 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, inc... | Glutamine amidotransferase |
c_o0z4xkd1zuza | 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 ... | Glutamine amidotransferase |
c_hww2a3d1ezjr | 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 ... | Glycoside hydrolase family 100 |
c_wpxlt1s9qorn | 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 ... | Glycoside hydrolase family 101 |
c_1ei9mhgp32pk | 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 ... | Glycoside hydrolase family 108 |
c_9n1e7iygyjz2 | 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 == | Glycoside hydrolase family 108 |
c_6k5t3g3eh3dv | 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 h... | Glycoside hydrolase family 13 |
c_wr8epcp3vqqt | 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 hydro... | Glycoside hydrolase family 13 |
c_21ol5z6yvjzk | 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 h... | Glycoside hydrolase family 15 |
c_jh1dmh42cxph | 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 ... | Glycoside hydrolase family 15 |
c_qqoohh3gh5x4 | 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. ... | Glycoside hydrolase family 15 |
c_jjxmyzh3yqtu | 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 h... | Glycoside hydrolase family 20 |
c_p9m1gwtmzhqk | 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-hexos... | Glycoside hydrolase family 20 |
c_ycsm4yip48b7 | 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 == | Glycoside hydrolase family 20 |
c_whzijzwjwvbq | 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 h... | Glycoside hydrolase family 22 |
c_w4ci8d7f685v | 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 pr... | Glycoside hydrolase family 22 |
c_rs3wlc83dl93 | 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 lysozyme... | Glycoside hydrolase family 22 |
c_ca0hvgllalom | 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 positio... | Glycoside hydrolase family 22 |
c_x3g1k41vw4fl | 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 o... | Glycoside hydrolase family 22 |
c_q9die8xrmh91 | 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 h... | Glycoside hydrolase family 24 |
c_e7m57yhd3dfu | 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 ... | Glycoside hydrolase family 24 |
c_qbqx15ucqeps | 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. | Glycoside hydrolase family 24 |
c_n42xbed1zjo0 | 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 == | Glycoside hydrolase family 24 |
c_l9va318oza5b | 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 h... | Glycoside hydrolase family 25 |
c_6u8z629lbkre | 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 co... | Glycoside hydrolase family 25 |
c_xyjgo3g1z56m | 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 h... | Glycoside hydrolase family 26 |
c_5zowzc7agsia | 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 galactoglucom... | Glycoside hydrolase family 26 |
c_v1638gbw7ocr | 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 h... | Glycoside hydrolase family 27 |
c_1d5xxy7k8qvp | 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... | Glycoside hydrolase family 27 |
c_utduhrvgy00v | 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 en... | Glycoside hydrolase family 27 |
c_t6zd06ypgswx | 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 euka... | Glycoside hydrolase family 27 |
c_tvxaxw47mj8u | 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 h... | Glycoside hydrolase family 28 |
c_889y5bh90dse | 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 (... | Glycoside hydrolase family 28 |
c_l1vo229crkck | 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 == | Glycoside hydrolase family 28 |
c_9cuozwa5npv6 | 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 h... | Glycoside hydrolase family 29 |
c_kszexkmtic7t | 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, cr... | Glycoside hydrolase family 29 |
c_pvoer6j8js0d | 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... | Glycoside hydrolase family 29 |
c_eiqdhdoynnz5 | 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 hy... | Glycoside hydrolase family 3 |
c_a5qxy8fwqqyl | 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 h... | Glycoside hydrolase family 30 |
c_r0xtlk0q4hkd | 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,... | Glycoside hydrolase family 30 |
c_ql59r9yvf7zy | 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 h... | Glycoside hydrolase family 31 |
c_3anml3h90mcl | 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 h... | Glycoside hydrolase family 32 |
c_ct7pae8k6vml | 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 sandwi... | Glycoside hydrolase family 32 |
c_lpclsngc0cr5 | 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 h... | Glycoside hydrolase family 33 |
c_ygj7eojslzb5 | 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 an... | Glycoside hydrolase family 33 |
c_jl8bow6cq1h1 | 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 h... | Glycoside hydrolase family 35 |
c_o840tw0u0pk5 | 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 (gen... | Glycoside hydrolase family 35 |
c_ipoqdw4np17x | 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 h... | Glycoside hydrolase family 36 |
c_p2bcz7vkf4el | 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-ace... | Glycoside hydrolase family 36 |
c_0yq7fky10ppg | 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 en... | Glycoside hydrolase family 36 |
c_o81gnnn2wjfb | 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 euka... | Glycoside hydrolase family 36 |
c_4hpfr7pwfxg4 | 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 k... | Glycoside hydrolase family 36 |
c_s0i1phiiddmi | 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 h... | Glycoside hydrolase family 37 |
c_8za2djoq1v7s | 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 == | Glycoside hydrolase family 37 |
c_nl30l10ga4k7 | 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 h... | Glycoside hydrolase family 38 |
c_1iwcn1k8jm4n | 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 caus... | Glycoside hydrolase family 38 |
c_j0n6r1pccef6 | 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 == | Glycoside hydrolase family 38 |
c_1kjfh9ojixfo | 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 h... | Glycoside hydrolase family 39 |
c_hnu9a8yeckg4 | 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 == | Glycoside hydrolase family 39 |
c_qbtexromv58d | 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... | Glycoside hydrolase family 4 |
c_uxoo76c17jhf | 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 h... | Glycoside hydrolase family 42 |
c_86syp6oac0uo | 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 == | Glycoside hydrolase family 42 |
c_rzihwauaom6f | 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 h... | Glycoside hydrolase family 43 |
c_f9bckcltk43r | 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 == | Glycoside hydrolase family 43 |
c_n5sd4zaa7bb5 | 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 h... | Glycoside hydrolase family 44 |
c_s48h3qbedet4 | 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 over... | Glycoside hydrolase family 44 |
c_owrp8576crhm | 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 h... | Glycoside hydrolase family 45 |
c_l3t7kb4hx35s | 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.... | Glycoside hydrolase family 45 |
c_taln6zu0cl98 | 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 h... | Glycoside hydrolase family 46 |
c_h3tjm4idm3g0 | 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-l... | Glycoside hydrolase family 46 |
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