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Glucose is hydrolyzed on fully folded protein and the mannose moieties are hydrolyzed by ER and Golgi-resident mannosidases. Typically, mature human glycoproteins only contain three mannose residues buried under sequential modification by GlcNAc, galactose, and sialic acid.
Hydrolysis of terminal, non-reducing β-D-mannose residues in β-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism.
Mannose receptor knockout mice are less able to clear these proteins, and show increased concentrations of a number of lysosomal hydrolases in the blood. [ 5 ] Consistent with this function, the mannose receptor is expressed at low levels during inflammation and at high levels during the resolution of inflammation, to ensure inflammatory agents ...
Mannosidase is an enzyme which hydrolyses mannose. [1]There are two types: alpha-Mannosidase; beta-Mannosidase; A deficiency is associated with mannosidosis.. A family of mannosidases are also responsible for processing newly formed glycoproteins in the endoplasmic reticulum into mature glycoproteins containing highly heterogeneous complex-type glycans.
GDP-mannose is produced from GTP and mannose-6-phosphate by the enzyme mannose-1-phosphate guanylyltransferase. The degradation of mannans (and many related forms of hemicellulose) has been well studied. The hydrolysis of the main mannan backbone is catalyzed by various enzymes including β-mannosidase, β-glucosidase, and β-mannase.
Xyloglucan backbone synthesis is mediated by cellulose synthase-like protein family C (CSLC), particularly glucan synthase, which adds glucose units to the chain. [ 8 ] [ 9 ] Backbone synthesis of xyloglucan is also mediated in some way by xylosyltransferase , but this mechanism is separate to its transferase function and remains unclear. [ 9 ]
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