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In molecular biology, glycoside hydrolase family 47 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_47 |
Alpha-mannosidase is involved in the maturation of Asn-linked oligosaccharides. The enzyme hydrolyses terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide man(9)(glcnac)(2) in a calcium-dependent manner. The mannose residues are trimmed away to produce, first, man(8)glcnac(2), then a man(5)... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_47 |
In molecular biology, glycoside hydrolase family 48 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_48 |
An example of an enzyme containing a domain belonging to this family is one of the cellulases (celA) from the genome of the thermophilic anaerobic bacterium Caldocellum saccharolyticum. The celA gene product is a polypeptide of 1751 amino acids; this has a multidomain structure comprising two catalytic domains and two ... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_48 |
The N-terminal domain encodes an endoglucanase activity on carboxymethylcellulose, consistent with its similarity to several endo-1, 4-beta-D-glucanase sequences, and is a member of the glycoside hydrolase family 9. The C-terminal domain belongs to this family shows similarity to a cellulase from Clostridium thermocell... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_48 |
In molecular biology, glycoside hydrolase family 49 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_49 |
In molecular biology, glycoside hydrolase family 5 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_5 |
One of these families is known as the cellulase family A or as the glycosyl hydrolases family 5. One of the conserved regions in this family contains a conserved glutamic acid residue which is potentially involved in the catalytic mechanism. In a recent study using Molecular Dynamics simulations, a considerable correla... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_5 |
In molecular biology, glycoside hydrolase family 52 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_52 |
Proteins harboring beta-xylosidase and xylanase activities have been identified in the Gram-positive, facultative thermophilic aerobe Bacillus stearothermophilus 21. This microbe, which functions in xylan degradation, can utilise xylan as a sole source of carbon. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_52 |
The enzyme hydrolyses 1,4-beta-D-xylans, removing successive D-xylose residues from the non-reducing termini. It also hydrolyses xylobiose. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_52 |
In molecular biology, glycoside hydrolase family 56 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_56 |
The venom of Apis mellifera (Honeybee) contains several biologically-active peptides and two enzymes, one of which is a hyaluronidase. The amino acid sequence of bee venom hyaluronidase contains 349 amino acids, and includes four cysteines and a number of potential glycosylation sites. The sequence shows a high degree ... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_56 |
In molecular biology, glycoside hydrolase family 57 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_57 |
In molecular biology, glycoside hydrolase family 59 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_59 |
Globoid cell leukodystrophy (Krabbe disease) is a severe, autosomal recessive disorder that results from deficiency of galactocerebrosidase (GALC) activity. GALC is responsible for the lysosomal catabolism of certain galactolipids, including galactosylceramide and psychosine. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_59 |
In molecular biology, glycoside hydrolase family 6 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_6 |
The active site of CBHII is located at the C-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the centre of the tunnel are the probable catalytic residues. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_6 |
In molecular biology, glycoside hydrolase family 62 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_62 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.This is a family of alpha-L-arabinofuranosidases (EC 3.2.1.55) (CAZY GH_62). These enzymes hydrolyze aryl alpha-L-arabinofuranosides and cleaves arabinosyl side chains from arabi... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_62 |
In molecular biology, glycoside hydrolase family 63 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_63 |
They catalyse the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC 3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_63 |
In molecular biology, glycoside hydrolase family 65 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_65 |
Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. It consists of three structural domains. The C-terminal domain forms a two layered jelly roll motif. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_65 |
This domain is situated at the base of the catalytic domain, however its function remains unknown. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_65 |
The catalytic domain also forms the majority of the dimerisation interface. The N-terminal domain is believed to be essential for catalytic activity although its precise function remains unknown. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_65 |
In molecular biology, glycoside hydrolase family 66 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_66 |
In molecular biology, glycoside hydrolase family 67 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_67 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 67 includes alpha-glucuronidases, these are components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_67 |
Within this central domain, the invariant Glu and Asp (residues 391 and 364 respectively from Bacillus stearothermophilus) are thought to form the catalytic centre. The C-terminal region of alpha-glucuronidase is mainly alpha-helical. It wraps around the catalytic domain, making additional interactions both with the N-... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_67 |
In molecular biology, glycoside hydrolase family 68 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_68 |
Levansucrase (EC 2.4.1.10), also known as beta-D-fructofuranosyl transferase, catalyses the conversion of sucrose and (2,6-beta-D-fructosyl)(N) to glucose and (2,6-beta-D-fructosyl)(N+1), where other sugars can also act as fructosyl acceptors. Invertase, or extracellular sucrase (EC 3.2.1.26), catalyses the hydrolysis ... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_68 |
In molecular biology, glycoside hydrolase family 7 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_7 |
Structurally, cellulases and xylanases frequently consist of a catalytic domain joined to a cellulose-binding domain (CBD) via a linker region that is rich in proline and/or hydroxy-amino acids. In type I exoglucanases, the CBD domain is found at the C-terminal extremity of these enzyme (this short domain forms a hairp... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_7 |
In molecular biology, glycoside hydrolase family 70 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_70 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.This family includes glucosyltransferases or sucrose 6-glycosyl transferases (GTF-S) (EC 2.4.1.5CAZY GH_70) which catalyse the transfer of D-glucopyramnosyl units from sucrose on... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_70 |
In molecular biology, glycoside hydrolase family 71 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_71 |
In molecular biology, glycoside hydrolase family 72 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_72 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.This family includes yeast glycolipid proteins anchored to the membrane. It includes Candida albicans pH-regulated protein, which is required for apical growth and plays a role i... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_72 |
In molecular biology, glycoside hydrolase family 73 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_73 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 73 CAZY GH_73 includes peptidoglycan hydrolases with endo-β-N-acetylglucosaminidase specificity. Members of this family include mannosyl-glycoprotein e... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_73 |
In molecular biology, glycoside hydrolase family 75 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_75 |
This family includes several fungal chitosanase proteins. Chitin, xylan, 6-O-sulphated chitosan and O-carboxymethyl chitin are indigestible by chitosanase. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_75 |
In molecular biology, glycoside hydrolase family 76 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_76 |
In molecular biology, glycoside hydrolase family 77 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_77 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.The enzymes in this family have amylomaltase or 4-α-glucanotransferase activity (EC 2.4.1.25) CAZY GH_77, they transfer a segment of a (1,4)-alpha-D-glucan to a new 4-position in... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_77 |
In molecular biology, glycoside hydrolase family 78 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_78 |
This family includes bacterial rhamnosidase A and B enzymes. L-Rhamnose is abundant in biomass as a common constituent of glycolipids and glycosides, such as plant pigments, pectic polysaccharides, gums or biosurfactants. Some rhamnosides are important bioactive compounds. | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_78 |
For example, terpenyl glycosides, the glycosidic precursor of aromatic terpenoids, act as important flavouring substances in grapes. Other rhamnosides act as cytotoxic rhamnosylated terpenoids, as signal substances in plants or play a role in the antigenicity of pathogenic bacteria. == References == | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_78 |
In molecular biology, glycoside hydrolase family 79 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_79 |
Heparan sulphate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulphate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena inv... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_79 |
The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularisation, both critical steps in cancer progression. The enzyme is ... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_79 |
In molecular biology, glycoside hydrolase family 8 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_8 |
In molecular biology, glycoside hydrolase family 80 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_80 |
In molecular biology, glycoside hydrolase family 81 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_81 |
In molecular biology, glycoside hydrolase family 85 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_85 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 85 enzymes have endo-beta-N-acetylglucosaminidase activity EC 3.2.1.96 (CAZY GH_85). These enzymes work on a broad spectrum of substrates. == Reference... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_85 |
In molecular biology, glycoside hydrolase family 88 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_88 |
In molecular biology, glycoside hydrolase family 89 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_89 |
The enzyme consist of three structural domains, the N-terminal domain has an alpha-beta fold, the central domain has a TIM barrel fold, and the C-terminal domain has an all alpha helical fold.Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate. Mutations on the ... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_89 |
In molecular biology, glycoside hydrolase family 9 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_9 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 9 CAZY GH_9 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4) and cellobiohydrolase (EC 3.2.1.91). These enzymes wer... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_9 |
In molecular biology, glycoside hydrolase family 92 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_92 |
They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.Glycoside hydrolase family 92 includes enzymes with mannosyl-oligosaccharide α-1,2-mannosidase EC 3.2.1.113, mannosyl-oligosaccharide α-1,3-mannosidase EC 3.2.1.-, mannosyl-oligosaccharide α-1,6-mannosidase EC 3.2.1.-, α-man... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_92 |
In molecular biology, glycoside hydrolase family 97 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_97 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Glycoside hydrolase family 97 (GH97) is a bacterial family. The central part of the GH97 family protein sequences represents a typical and complete (beta/alpha)8-barrel or cataly... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_97 |
In molecular biology, glycoside hydrolase family 98 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... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_98 |
This classification is available on the CAZy web site, and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.Members of glycoside hydrolase family 98 have endo-β-galactosidase activity. This family includes E-ABase from Clostridium perfringens which cleaves both blood group A and B glyc... | https://en.wikipedia.org/wiki/Glycoside_hydrolase_family_98 |
In molecular biology, group II pyridoxal-dependent decarboxylases are family of enzymes including aromatic-L-amino-acid decarboxylase (L-dopa decarboxylase or tryptophan decarboxylase) EC 4.1.1.28, which catalyses the decarboxylation of tryptophan to tryptamine, tyrosine decarboxylase EC 4.1.1.25, which converts tyrosi... | https://en.wikipedia.org/wiki/Group_II_pyridoxal-dependent_decarboxylases |
In molecular biology, group III pyridoxal-dependent decarboxylases are a family of bacterial enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18 and arginine decarboxylase EC 4.1.1.19.Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on... | https://en.wikipedia.org/wiki/Group_III_pyridoxal-dependent_decarboxylases |
In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family. ... | https://en.wikipedia.org/wiki/Group_IV_pyridoxal-dependent_decarboxylases |
Group IV comprises eukaryotic ornithine and lysine decarboxylase and the prokaryotic biosynthetic type of arginine decarboxylase and diaminopimelate decarboxylase.Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. The proteins contain a conserved ly... | https://en.wikipedia.org/wiki/Group_IV_pyridoxal-dependent_decarboxylases |
In molecular biology, heat shock factors (HSF), are the transcription factors that regulate the expression of the heat shock proteins. A typical example is the heat shock factor of Drosophila melanogaster. | https://en.wikipedia.org/wiki/Heat_Shock_Factor |
In molecular biology, holdases are a particular kind of molecular chaperones that assist the non-covalent folding of proteins in an ATP-independent manner. Examples of holdases are DnaJ and Hsp33. Holdases bind to protein folding intermediates to prevent their aggregation but without directly refolding them. They stand... | https://en.wikipedia.org/wiki/Holdase |
In molecular biology, housekeeping genes are typically constitutive genes that are required for the maintenance of basic cellular function, and are expressed in all cells of an organism under normal and patho-physiological conditions. Although some housekeeping genes are expressed at relatively constant rates in most n... | https://en.wikipedia.org/wiki/Housekeeping_genes |
The key criterion for the use of a housekeeping gene in this manner is that the chosen housekeeping gene is uniformly expressed with low variance under both control and experimental conditions. Validation of housekeeping genes should be performed before their use in gene expression experiments such as RT-PCR. Recently ... | https://en.wikipedia.org/wiki/Housekeeping_genes |
In molecular biology, hybridization (or hybridisation) is a phenomenon in which single-stranded deoxyribonucleic acid (DNA) or ribonucleic acid (RNA) molecules anneal to complementary DNA or RNA. Though a double-stranded DNA sequence is generally stable under physiological conditions, changing these conditions in the l... | https://en.wikipedia.org/wiki/Nucleic_acid_hybridisation |
In molecular biology, hydroxymethylglutaryl-CoA synthase or HMG-CoA synthase EC 2.3.3.10 is an enzyme which catalyzes the reaction in which acetyl-CoA condenses with acetoacetyl-CoA to form 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA). This reaction comprises the second step in the mevalonate-dependent isoprenoid biosynthe... | https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_synthase |
This results in shunting of excess acetyl-CoA into the ketone synthesis pathway via HMG-CoA, leading to the development of diabetic ketoacidosis. The 3 substrates of this enzyme are acetyl-CoA, H2O, and acetoacetyl-CoA, whereas its two products are (S)-3-hydroxy-3-methylglutaryl-CoA and CoA. In humans, the protein is e... | https://en.wikipedia.org/wiki/Hydroxymethylglutaryl-CoA_synthase |
In molecular biology, insertional mutagenesis is the creation of mutations in DNA by the addition of one or more base pairs. Such insertional mutations can occur naturally, mediated by viruses or transposons, or can be artificially created for research purposes in the lab. | https://en.wikipedia.org/wiki/Insertional_mutagenesis |
In molecular biology, intercellular adhesion molecules (ICAMs) and vascular cell adhesion molecule-1 (VCAM-1) are part of the immunoglobulin superfamily. They are important in inflammation, immune responses and in intracellular signalling events. The ICAM family consists of five members, designated ICAM-1 to ICAM-5. | https://en.wikipedia.org/wiki/Intercellular_adhesion_molecule |
They are known to bind to leucocyte integrins CD11/CD18 such as LFA-1 and Macrophage-1 antigen, during inflammation and in immune responses. In addition, ICAMs may exist in soluble forms in human plasma, due to activation and proteolysis mechanisms at cell surfaces. Mammalian intercellular adhesion molecules include: I... | https://en.wikipedia.org/wiki/Intercellular_adhesion_molecule |
In molecular biology, kanamycin nucleotidyltransferase EC 2.7.7.- (KNTase) is an enzyme which is involved in conferring resistance to aminoglycoside antibiotics. It catalyses the transfer of a nucleoside monophosphate group from a nucleotide to kanamycin. This enzyme is dimeric with each subunit being composed of two d... | https://en.wikipedia.org/wiki/Kanamycin_nucleotidyltransferase |
The C-terminal domain contains five alpha helices, four of which are organised into an up-and-down alpha helical bundle. Residues found in this domain may contribute to this enzyme's active site. == References == | https://en.wikipedia.org/wiki/Kanamycin_nucleotidyltransferase |
In molecular biology, linker DNA is double-stranded DNA (38-53 base pairs long) in between two nucleosome cores that, in association with histone H1, holds the cores together. Linker DNA is seen as the string in the "beads and string model", which is made by using an ionic solution on the chromatin. Linker DNA connects... | https://en.wikipedia.org/wiki/Linker_DNA |
Linker DNA may be degraded by endonucleases.The linkers are short double stranded DNA segments which are formed of oligonucleotides. These contain target sites for the action of one or more restriction enzymes. The linkers can be synthesized chemically and can be ligated to the blunt end of foreign DNA or vector DNA. T... | https://en.wikipedia.org/wiki/Linker_DNA |
In molecular biology, members of the ArgJ protein family are bifunctional protein that catalyses the first (EC 2.3.1.35) and fifth steps (EC 2.3.1.1) in arginine biosynthesis. The structure has been determined for glutamate N-acetyltransferase 2 (ornithine acetyltransferase), an ArgJ-like protein from Streptomyces clav... | https://en.wikipedia.org/wiki/ArgJ_protein_family |
In molecular biology, members of the KIN2/PAR-1/MARK kinase family of proteins are kinases that are conserved from yeast to human and share the same domain organisation: an N-terminal kinase domain and a C-terminal kinase associated domain 1 (KA1). Some members of this family also contain an UBA domain (ubiquitin-assoc... | https://en.wikipedia.org/wiki/KIN2/PAR-1/MARK_kinase_family |
Some proteins known to contain a KA1 domain are listed below: Mammalian MAP/microtubule affinity-regulating kinases (MARK 1, 2, 3). They regulate polarity in neuronal cell models and appear to function redundantly in phosphorylating microtubule-associated proteins and in regulating microtubule stability. Mammalian mate... | https://en.wikipedia.org/wiki/KIN2/PAR-1/MARK_kinase_family |
It phosphorylates ZNF622 and may contribute to its redirection to the nucleus. It may be involved in the inhibition of spliceosome assembly during mitosis. Caenorhabditis elegans and Drosophila PAR-1 protein, required for establishing polarity in embryos where it is asymmetrically distributed. | https://en.wikipedia.org/wiki/KIN2/PAR-1/MARK_kinase_family |
Fungal Kin1 and Kin2 protein kinases involved in regulation of exocytosis. They localise to the cytoplasmic face of the plasma membrane. Plant KIN10 and KIN11 proteins, catalytic subunits of the putative trimeric SNF1-related protein kinase (SnRK) complex. == References == | https://en.wikipedia.org/wiki/KIN2/PAR-1/MARK_kinase_family |
In molecular biology, messenger ribonucleic acid (mRNA) is a single-stranded molecule of RNA that corresponds to the genetic sequence of a gene, and is read by a ribosome in the process of synthesizing a protein. mRNA is created during the process of transcription, where an enzyme (RNA polymerase) converts the gene int... | https://en.wikipedia.org/wiki/Monocistronic_mRNA |
This exon sequence constitutes mature mRNA. Mature mRNA is then read by the ribosome, and, utilising amino acids carried by transfer RNA (tRNA), the ribosome creates the protein. This process is known as translation. | https://en.wikipedia.org/wiki/Monocistronic_mRNA |
All of these processes form part of the central dogma of molecular biology, which describes the flow of genetic information in a biological system. As in DNA, genetic information in mRNA is contained in the sequence of nucleotides, which are arranged into codons consisting of three ribonucleotides each. Each codon code... | https://en.wikipedia.org/wiki/Monocistronic_mRNA |
The translation of codons into amino acids requires two other types of RNA: transfer RNA, which recognizes the codon and provides the corresponding amino acid, and ribosomal RNA (rRNA), the central component of the ribosome's protein-manufacturing machinery. The concept of mRNA was developed by Sydney Brenner and Franc... | https://en.wikipedia.org/wiki/Monocistronic_mRNA |
In molecular biology, methylation induced premeiotically (MIP) is a process by which cytosines within repeated DNA sequences are de novo methylated prior to the sexual cycle. This process was first described in the ascomycete Ascobolus immersens. MIP is dependent upon the gene masc1 which encodes a cytosine methyltrans... | https://en.wikipedia.org/wiki/Methylation_induced_premeiotically |
At least one major function of the process appears to be genome defense. Related functions have been found in other fungi, including Neurospora and Aspergillus species. == References == | https://en.wikipedia.org/wiki/Methylation_induced_premeiotically |
In molecular biology, miR-130 microRNA precursor is a small non-coding RNA that regulates gene expression. This microRNA has been identified in mouse (MI0000156, MI0000408), and in human (MI0000448, MI0000748). miR-130 appears to be vertebrate-specific miRNA and has now been predicted or experimentally confirmed in a r... | https://en.wikipedia.org/wiki/Mir-130_microRNA_precursor_family |
In this case, the mature sequence is excised from the 3' arm of the hairpin. It has been found that miR-130 is upregulated in a type of cancer called hepatocellular carcinoma. It has been shown that miR-130a is expressed in the hematopoietic stem/progenitor cell compartment but not in mature blood cells. | https://en.wikipedia.org/wiki/Mir-130_microRNA_precursor_family |
In molecular biology, miR-148 is a microRNA whose expression has been demonstrated in human (MI0000253), mouse (MI0000550), rat (MI0000616) and zebrafish (MI0002015). miR-148 has also been predicted in chicken (MI0001189). These predicted hairpin precursor sequence are related to those of miR-152, which has been expres... | https://en.wikipedia.org/wiki/Mir-148/mir-152_microRNA_precursor_family |
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