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An acid hydrolase is an enzyme that works best at acidic pHs.It is commonly located in lysosomes, which are acidic on the inside.Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the approximately 50 degradative enzymes of the lysosome that break apart biological matter.
The lysosomal membrane protects the cytosol, and therefore the rest of the cell, from the degradative enzymes within the lysosome. The cell is additionally protected from any lysosomal acid hydrolases that drain into the cytosol, as these enzymes are pH-sensitive and do not function well or at all in the alkaline environment of the cytosol ...
Hydrolases are classified as EC 3 in the EC number classification of enzymes. Hydrolases can be further classified into several subclasses, based upon the bonds they act upon: EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase) EC 3.2: sugars (DNA glycosylases, glycoside hydrolase) EC 3.3: ether bonds
[2] [3] The larger receptor is known as the cation-independent mannose 6-phosphate receptor , while the smaller receptor requires divalent cations to efficiently recognize lysosomal hydrolases. [3] While divalent cations are not essential for ligand binding by the human CD-MPR, the nomenclature has been retained. [4]
Deficiency in specific lysosomal glycoside hydrolases can lead to a range of lysosomal storage disorders that result in developmental problems or death. Glycoside hydrolases are found in the intestinal tract and in saliva where they degrade complex carbohydrates such as lactose, starch, sucrose and trehalose.
GlcNAc-1-phosphotransferase functions to prepare newly made enzymes for lysosome transportation (lysosomal hydrolases to the lysosome). Lysosomes, a part of an animal cell, helps break down large molecules into smaller ones that can be reused. GlcNAc-1-phosphotransferase phosphorylates carbon 6 of one or more mannosyl residues of N linked ...
Glycoside hydrolases (O-Glycosyl 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 glycosyl hydrolases, based on sequence similarity, has led to the definition of numerous different ...
Each saposin has an α-helical structure that is seen as being important for stimulation because this structure is maximal at a pH of 4.5; which is optimal for many lysosomal hydrolases. [7] This helical structure is seen in all (especially with the first region), but saposin has been predicted to have β-sheet configuration due to it first 24 ...
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