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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.
One katal is the enzyme activity that converts one mole of substrate per second under specified assay conditions, so 1 U = 1 μmol/min = 1/60 μmol/s ≈ 16.67 nmol/s; 16.67 nkat = 16.67 nmol/s; Therefore, 1 U = 16.67 nkat [4] While the katal may be recommended, almost all scientific research today still uses the system based on the minute, for ...
Hydrogen bonding and electrostatic interactions are shown by green dashed lines. All green dashes represent distances of less than 3.7 Å. G6PD is generally found as a dimer of two identical monomers (see main thumbnail). [8] Depending on conditions, such as pH, these dimers can themselves dimerize to form tetramers. [5]
3). Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
The enzyme maintains acid-base balance and helps ... and tissues because the pKa is close to the physiological pH = 7.2 – 7.6. Since HCO 3 ... 3.1 × 10 5: 41 CA ...
Endohydrolysis of (1→4)-α-D-glucosidic linkages in polysaccharides containing three or more (1→4)-α-linked D-glucose units. It is the major form of amylase found in humans and other mammals. [3] It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. It is a member of glycoside hydrolase family 13.
N-acetyl-β-d-glucosaminidase (EC 3.2.1.30; EC 3.2.1.52) is a mesophilic hydrolase that specifically hydrolyzes N-acetyl-glucosides. The enzyme is found across a wide variety of marine and terrestrial creatures with the primary function of breaking down oligosaccharides in the presence of water.
[11] [12] Accordingly, its primary site of synthesis and activity is in the stomach (pH 1.5 to 2). In humans the concentration of pepsin in the stomach reaches 0.5 – 1 mg/mL. [13] [14] Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0.