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c_fqii5suv8ln4 | 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 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 47 CAZY GH_47 comprises enzymes with only one known activity; alpha-mannosidase (EC 3.2.1.113). | Glycoside hydrolase family 47 |
c_xt37f7kg7tmx | 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)(glcnac)(2) structure. == References == | Glycoside hydrolase family 47 |
c_fhh7mwhhmhc4 | 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 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 48 CAZY GH_48 comprises enzymes with several known activities; endoglucanase (EC 3.2.1.4); cellobiohydrolase (EC 3.2.1.91). | Glycoside hydrolase family 48 |
c_4t5g5zkr0gov | 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 cellulose-binding domains, linked by Pro-Thr-rich regions. | Glycoside hydrolase family 48 |
c_pavf5jeaf0td | 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 thermocellum (CelS), which acts synergistically with a second component to hydrolyse crystalline cellulose. == References == | Glycoside hydrolase family 48 |
c_su5m7zp2kods | 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 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 49 is a family of dextranases and isopullulanases. Dextranase hydrolyses alpha-1,6-glycosidic bonds in dextran polymers. | Glycoside hydrolase family 49 |
c_l7db1trtk7zp | 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 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 5 CAZY GH_5 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4); beta-mannanase (EC 3.2.1.78); exo-1,3-glucanase (EC 3.2.1.58); endo-1,6-glucanase (EC 3.2.1.75); xylanase (EC 3.2.1.8); endoglycoceramidase (EC 3.2.1.123); xanthanase.The microbial degradation of cellulose and xylans requires several types of enzymes. Fungi and bacteria produces a spectrum of cellulolytic enzymes (cellulases) and xylanases which, on the basis of sequence similarities, can be classified into families. | Glycoside hydrolase family 5 |
c_hb46wsxp54u6 | 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 correlation between thermal stability and structural rigidity of members of family 5 with solved structures has been proved. | Glycoside hydrolase family 5 |
c_yfovprrotw36 | 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 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 52 CAZY GH_52 comprises enzymes with only one known activity; beta-xylosidase (EC 3.2.1.37). | Glycoside hydrolase family 52 |
c_jc11drnm7p4b | 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. | Glycoside hydrolase family 52 |
c_rtgwofhdqtij | The enzyme hydrolyses 1,4-beta-D-xylans, removing successive D-xylose residues from the non-reducing termini. It also hydrolyses xylobiose. == References == | Glycoside hydrolase family 52 |
c_akx0gswfw6vs | 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 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 56 CAZY GH_56 includes enzymes with hyaluronidase EC 3.2.1.35 activity. | Glycoside hydrolase family 56 |
c_01abkjxxjr1k | 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 of similarity to PH-20, a membrane protein of mammalian sperm involved in sperm-egg adhesion, supporting the view that hyaluronidases play a role in fertilisation.PH-20 is required for sperm adhesion to the egg zona pellucida; it is located on both the sperm plasma membrane and acrosomal membrane. The amino acid sequence of the mature protein contains 468 amino acids, and includes six potential N-linked glycosylation sites and twelve cysteines, eight of which are tightly clustered near the C-terminus. == References == | Glycoside hydrolase family 56 |
c_kyq6t500w8vq | 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 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 57 CAZY GH_57 comprises enzymes with several known activities; alpha-amylase (EC 3.2.1.1), 4-alpha-glucanotransferase (EC 2.4.1.25), α-galactosidase (EC 3.2.1.22); amylopullulanase (EC 3.2.1.41); branching enzyme (EC 2.4.1.18). It includes a thermostable alpha-amylase with a broad substrate specificity from the archaebacterium Pyrococcus furiosus. | Glycoside hydrolase family 57 |
c_wnv8yp26l53i | 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 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 59 CAZY GH_59 comprises enzymes with only one known activity; galactocerebrosidase (EC 3.2.1.46). | Glycoside hydrolase family 59 |
c_4srx86mlbuoq | 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 == | Glycoside hydrolase family 59 |
c_rn5x7wnmyoq2 | 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 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 6 CAZY GH_6 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4) and cellobiohydrolase (EC 3.2.1.91). These enzymes were formerly known as cellulase family B. The 3D structure of the enzymatic core of cellobiohydrolase II (CBHII) from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to the ubiquitous barrel topology first seen in triose phosphate isomerase. | Glycoside hydrolase family 6 |
c_5axfyhidxqah | 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 == | Glycoside hydrolase family 6 |
c_zdo1ze8bki0g | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 62 |
c_doq5p1lde1qq | 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 arabinoxylan and arabinan. == References == | Glycoside hydrolase family 62 |
c_819tnm17qj61 | 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 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.Glycosyl hydrolase family 63 (CAZY GH_63) is a family of eukaryotic enzymes. | Glycoside hydrolase family 63 |
c_vezvoey0eyjv | 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 == | Glycoside hydrolase family 63 |
c_aukni5171l8f | 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 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 of glycosyl hydrolases (CAZY GH_65) includes vacuolar acid trehalase and maltose phosphorylases. | Glycoside hydrolase family 65 |
c_ghlniz327uxk | 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. | Glycoside hydrolase family 65 |
c_c6s67xbj68ch | 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 carbon atom. | Glycoside hydrolase family 65 |
c_wdsjis87k0pa | 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 == | Glycoside hydrolase family 65 |
c_qcyeycom0mjt | 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 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 66 CAZY GH_66 includes enzymes with cycloisomaltooligosaccharide glucanotransferase EC 2.4.1.248 and dextranase EC 3.2.1.11 activities. == References == | Glycoside hydrolase family 66 |
c_lgj6o525b0gk | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 67 |
c_cvjmxusxt0su | 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-1,2 linked 4-O-methyl glucuronic acid from xylans. Members of this family consist of three structural domains. Deletion mutants of alpha-glucuronidase from Bacillus stearothermophilus have indicated that the central region is responsible for the catalytic activity. | Glycoside hydrolase family 67 |
c_w69qz3rju7le | 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-terminal domain of its parent monomer and also forming the majority of the dimer-surface with the equivalent C-terminal domain of the other monomer of the dimer. == References == | Glycoside hydrolase family 67 |
c_d8342jpkm04s | 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 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 68 family (CAZY GH_68) includes several bacterial levansucrase enzymes, and invertase from Zymomonas. | Glycoside hydrolase family 68 |
c_y7lke51d6qxx | 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 of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranosides. == References == | Glycoside hydrolase family 68 |
c_qvsah0r0955c | 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 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 7 CAZY GH_7 comprises enzymes with several known activities including endoglucanase (EC 3.2.1.4) and cellobiohydrolase (EC 3.2.1.91). These enzymes were formerly known as cellulase family C. Exoglucanases and cellobiohydrolases play a role in the conversion of cellulose to glucose by cutting the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. | Glycoside hydrolase family 7 |
c_el3p0r19mcc0 | 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 hairpin loop structure stabilised by 2 disulphide bridges). == References == | Glycoside hydrolase family 7 |
c_jd9c30ytxber | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 70 |
c_6p4v8a7bo1jh | 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 onto acceptor molecules. Some members of this family contain a cell wall-binding repeat. == References == | Glycoside hydrolase family 70 |
c_8n2a128uesbd | 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 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.It is a family of alpha-1,3-glucanases (EC 3.2.1.59) (CAZY GH_71). == References == | Glycoside hydrolase family 71 |
c_k7ldy29ueb7g | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 72 |
c_jb77kb6uctxj | 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 in morphogenesis, and Saccharomyces cerevisiae glycolipid anchored surface protein. == References == | Glycoside hydrolase family 72 |
c_u5y13qe4mvs4 | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 73 |
c_ionshemln8a2 | 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 endo-beta-N-acetylglucosamidase EC 3.2.1.96 and flagellar protein J (flgJ), which has been shown to hydrolyse peptidoglycan. == References == | Glycoside hydrolase family 73 |
c_s7wajtzobg5m | 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 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 75 CAZY GH_75 includes enzymes with chitosanase EC 3.2.1.132 activity. | Glycoside hydrolase family 75 |
c_5578nlaohdk4 | This family includes several fungal chitosanase proteins. Chitin, xylan, 6-O-sulphated chitosan and O-carboxymethyl chitin are indigestible by chitosanase. == References == | Glycoside hydrolase family 75 |
c_seisuanm2hy5 | 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 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 76 is a family of alpha-1,6-mannanases (EC 3.2.1.101) (CAZY GH_76). == References == | Glycoside hydrolase family 76 |
c_8fsaqc5g4jx5 | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 77 |
c_uib4wtrm8l7j | 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 an acceptor, which may be glucose or (1,4)-alpha-D-glucan. They belong to the disproportionating family of enzymes. == References == | Glycoside hydrolase family 77 |
c_bmytcfeauk2f | 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 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 78 CAZY GH_78 includes enzymes with α-L-rhamnosidase EC 3.2.1.40 activity. | Glycoside hydrolase family 78 |
c_z3u80bf3p3ge | 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. | Glycoside hydrolase family 78 |
c_xwd1vqkccb2p | 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 == | Glycoside hydrolase family 78 |
c_9j14sdk9y4f0 | 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 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 79 includes endo-beta-N-glucuronidase EC 3.2.1.31 and heparanase (CAZY GH_79). | Glycoside hydrolase family 79 |
c_qblic41msczs | 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 involving cell migration and response to changes in the extracellular microenvironment. Heparanase degrades HS at specific intrachain sites. | Glycoside hydrolase family 79 |
c_p9hw978wpj00 | 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 also involved in cell migration associated with inflammation and autoimmunity. == References == | Glycoside hydrolase family 79 |
c_o13r9le1172w | 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 on sequence similarity, has led to the definition of >100 different families. This classification is available on the CAZy website, and also discussed at CAZypedia, an online encyclopedia of carbohydrate-active enzymes.Glycoside hydrolase family 8 CAZY GH_8 comprises enzymes with several known activities; endoglucanase (EC 3.2.1.4); lichenase (EC 3.2.1.73); chitosanase (EC 3.2.1.132). These enzymes were formerly known as cellulase family D. == References == | Glycoside hydrolase family 8 |
c_0a3h6oyl5lv6 | 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 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 80 CAZY GH_80 includes enzymes with chitosanase EC 3.2.1.132 activity. == References == | Glycoside hydrolase family 80 |
c_4smrb17ksnw2 | 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 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 81 is a family of eukaryotic beta-1,3-glucanases EC 3.2.1.39 (CAZY GH_81). == References == | Glycoside hydrolase family 81 |
c_9oft94ezx9ll | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 85 |
c_ohaz53r9oljg | 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. == References == | Glycoside hydrolase family 85 |
c_7kke6cmhqgp4 | 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 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 88 CAZY GH_88 includes enzymes with d-4,5 unsaturated β-glucuronyl hydrolase activity. == References == | Glycoside hydrolase family 88 |
c_sqavegmdwqk2 | 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 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 89 CAZY GH_89 includes enzymes with α-N-acetylglucosaminidase EC 3.2.1.50 activity. | Glycoside hydrolase family 89 |
c_f5taq2cid549 | 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 alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterised by neurological dysfunction but relatively mild somatic manifestations. == References == | Glycoside hydrolase family 89 |
c_mlolx5nkvyro | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 9 |
c_m0hjzhq0b0dd | 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 were formerly known as cellulase family E. Cellulases (Endoglucanases) EC 3.2.1.4 catalyse the endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose. GH9 family members have also been found in green microalgae (Chlamydomonas, Gonium and Volvox) that show highest sequence identity to endogenous GH9 cellulases from invertebrate metazoans == References == | Glycoside hydrolase family 9 |
c_jrhrcee3l9kq | 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 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 domain occurs within alpha-1,2-mannosidases, which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. | Glycoside hydrolase family 92 |
c_6qa32gnj8vea | 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-mannosidase EC 3.2.1.24, α-1,2-mannosidase EC 3.2.1.-, α-1,3-mannosidase EC 3.2.1.- and α-1,4-mannosidase EC 3.2.1.- activities. It includes enzymes critical for the maturation of N-linked oligosaccharides and ER-associated degradation. == References == | Glycoside hydrolase family 92 |
c_p52iup0r3fdr | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 97 |
c_qzc88vlfu0zu | 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 catalytic TIM-barrel type domain. The N- and C-terminal parts of the sequences, mainly consisting of beta-strands, most probably form two additional non-catalytic domains with as yet unknown functions. The non-catalytic domains of glycosidases from the alpha-galactosidase and alpha-glucosidase superfamilies are also predominantly composed of beta-strands, and at least some of these domains are involved in oligomerisation and carbohydrate binding. In all known glycosidases with the (beta-alpha)8-barrel fold, the amino acid residues at the active site are located on the C-termini of the beta-strands. | Glycoside hydrolase family 97 |
c_fkyponm7fy4g | 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 hydrolases, based on sequence similarity, has led to the definition of >100 different families. | Glycoside hydrolase family 98 |
c_peikzlzz2xhi | 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 glycotopes.The putative catalytic domain is found to the N-terminus of a second domain, which is not expected to form part of the catalytic activity. == References == | Glycoside hydrolase family 98 |
c_45gc0gamj8dd | 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 tyrosine into tyramine and histidine decarboxylase EC 4.1.1.22, which catalyses the decarboxylation of histidine to histamine.Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. Group II includes glutamate, histidine, tyrosine, and aromatic-L-amino-acid decarboxylases. | Group II pyridoxal-dependent decarboxylases |
c_1lj2le299y2z | 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 amino acid sequence. Group III comprises prokaryotic ornithine and lysine decarboxylase and the prokaryotic biodegradative type of arginine decarboxylase. | Group III pyridoxal-dependent decarboxylases |
c_ayhp6bla4w0x | 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. Pyridoxal-5'-phosphate-dependent amino acid decarboxylases can be divided into four groups based on amino acid sequence. | Group IV pyridoxal-dependent decarboxylases |
c_gthjfvxb8fmy | 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 lysine residue which is known, in mouse ODC to be the site of attachment of the pyridoxal-phosphate group. The proteins also contain a stretch of three consecutive glycine residues and has been proposed to be part of a substrate-binding region. | Group IV pyridoxal-dependent decarboxylases |
c_32fr7i1ps2xp | 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. | Heat Shock Factor |
c_pzap6ei9ca2f | 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 in opposition to foldases, which are chaperones that use ATP to fold proteins. | Holdase |
c_sa4965goej23 | 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 non-pathological situations, the expression of other housekeeping genes may vary depending on experimental conditions.The origin of the term "housekeeping gene" remains obscure. Literature from 1976 used the term to describe specifically tRNA and rRNA. For experimental purposes, the expression of one or multiple housekeeping genes is used as a reference point for the analysis of expression levels of other genes. | Housekeeping genes |
c_o72xo40jmdc8 | 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 a web-based database of human and mouse housekeeping genes and reference genes/transcripts, named Housekeeping and Reference Transcript Atlas (HRT Atlas), was developed to offer updated list of housekeeping genes and reliable candidate reference genes/transcripts for RT-qPCR data normalization. This database can be accessed at http://www.housekeeping.unicamp.br. | Housekeeping genes |
c_5t6xsqmmlfho | 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 laboratory (generally by raising the surrounding temperature) will cause the molecules to separate into single strands. These strands are complementary to each other but may also be complementary to other sequences present in their surroundings. Lowering the surrounding temperature allows the single-stranded molecules to anneal or “hybridize” to each other. DNA replication and transcription of DNA into RNA both rely upon nucleotide hybridization, as do molecular biology techniques including Southern blots and Northern blots, the polymerase chain reaction (PCR), and most approaches to DNA sequencing. | Nucleic acid hybridisation |
c_rba4y8ry4gkn | 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 biosynthesis pathway. HMG-CoA is an intermediate in both cholesterol synthesis and ketogenesis. This reaction is overactivated in patients with diabetes mellitus type 1 if left untreated, due to prolonged insulin deficiency and the exhaustion of substrates for gluconeogenesis and the TCA cycle, notably oxaloacetate. | Hydroxymethylglutaryl-CoA synthase |
c_ki3z8ljion9i | 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 encoded by the HMGCS1 gene on chromosome 5. | Hydroxymethylglutaryl-CoA synthase |
c_4p3moj1x0uz9 | 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. | Insertional mutagenesis |
c_vz0wdvngwjx5 | 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. | Intercellular adhesion molecule |
c_dqocdn684y11 | 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: ICAM-1 ICAM2 ICAM3 ICAM4 ICAM5 == References == | Intercellular adhesion molecule |
c_00134s259ala | 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 domains. | Kanamycin nucleotidyltransferase |
c_06dbh0ra9ntr | 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 == | Kanamycin nucleotidyltransferase |
c_08bua3r1fnzk | 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 to histone H1 and histone H1 sits on the nucleosome core. Nucleosome is technically the consolidation of a nucleosome core and one adjacent linker DNA; however, the term nucleosome is used freely for solely the core. | Linker DNA |
c_qtogxmk84fza | 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. These are then treated with restriction endonuclease enzyme to produce cohesive ends of DNA fragments. The commonly used linkers are EcoRI-linkers and sal-I linkers. | Linker DNA |
c_zmlylmxb9120 | 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 clavuligerus. == References == | ArgJ protein family |
c_ahyew8i1ouwf | 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-associated domain). Members of this kinase family are involved in various biological processes such as cell polarity, cell cycle control, intracellular signalling, microtubule stability and protein stability. The function of the KA1 domain is not yet known. | KIN2/PAR-1/MARK kinase family |
c_hxb443hl385m | 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 maternal embryonic leucine zipper kinase (MELK). | KIN2/PAR-1/MARK kinase family |
c_4oz7s5450hjy | 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. | KIN2/PAR-1/MARK kinase family |
c_jizy5o6ziisi | 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 == | KIN2/PAR-1/MARK kinase family |
c_q01q8oiheax9 | 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 into primary transcript mRNA (also known as pre-mRNA). This pre-mRNA usually still contains introns, regions that will not go on to code for the final amino acid sequence. These are removed in the process of RNA splicing, leaving only exons, regions that will encode the protein. | Monocistronic mRNA |
c_fypbvy5rpsyp | 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. | Monocistronic mRNA |
c_ccj7jt9ds6qq | 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 codes for a specific amino acid, except the stop codons, which terminate protein synthesis. | Monocistronic mRNA |
c_6cw3zj31651i | 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 Francis Crick in 1960 during a conversation with François Jacob. In 1961, mRNA was identified and described independently by one team consisting of Brenner, Jacob, and Matthew Meselson, and another team led by James Watson. While analyzing the data in preparation for publication, Jacob and Jacques Monod coined the name "messenger RNA". | Monocistronic mRNA |
c_26x428crl0y6 | 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 methyltransferase-like protein. | Methylation induced premeiotically |
c_xvran7gqtfg8 | 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 == | Methylation induced premeiotically |
c_f3wo5c4b2om0 | 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 range of vertebrate species (MIPF0000034). Mature microRNAs are processed from the precursor stem-loop by the Dicer enzyme. | Mir-130 microRNA precursor family |
c_mqwiozlsxuy9 | 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. | Mir-130 microRNA precursor family |
c_hbl438gio6ka | 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 expressed in mouse (MI0000174) and is predicted in human (MI0000462).The hairpin precursors (represented here) are predicted based on base pairing and cross-species conservation; their extents are not known. In this case, the mature sequence is excised from the 3' arm of the hairpin. | Mir-148/mir-152 microRNA precursor family |
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