Search results
Results from the WOW.Com Content Network
Disaccharidases are glycoside hydrolases, enzymes that break down certain types of sugars called disaccharides into simpler sugars called monosaccharides.In the human body, disaccharidases are made mostly in an area of the small intestine's wall called the brush border, making them members of the group of "brush border enzymes".
Excessive flatus and abdominal bloating may reflect excessive gas production due to fermentation of unabsorbed carbohydrate, especially among patients with a primary or secondary disaccharidase deficiency, such as lactose intolerance or sucrose intolerance. Malabsorption of dietary nutrients and excessive fluid secretion by inflamed small ...
Sucrose intolerance or genetic sucrase-isomaltase deficiency (GSID) is the condition in which sucrase-isomaltase, an enzyme needed for proper metabolism of sucrose (sugar) and starch (e.g., grains), is not produced or the enzyme produced is either partially functional or non-functional in the small intestine. All GSID patients lack fully ...
Glycogen storage diseases that affect the liver typically cause hepatomegaly and hypoglycemia; those that affect skeletal muscle cause exercise intolerance, progressive weakness and cramping. [1] Glucose-6-phosphate isomerase deficiency affects step 2 of glycolysis. Triosephosphate isomerase deficiency affects step 5 of glycolysis.
There are two functionally different classes of disaccharides: Reducing disaccharides, in which one monosaccharide, the reducing sugar of the pair, still has a free hemiacetal unit that can perform as a reducing aldehyde group; lactose, maltose and cellobiose are examples of reducing disaccharides, each with one hemiacetal unit, the other occupied by the glycosidic bond, which prevents it from ...
Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!
Some FODMAPs, such as fructose, are readily absorbed in the small intestine of humans via GLUT receptors. [19] Absorption thus depends on the appropriate expression and delivery of these receptors in the intestinal enterocyte to both the apical surface, contacting the lumen of the intestine (e.g., GLUT5), and to the basal membrane, contacting the blood (e.g., GLUT2). [19]
Sucrase-isomaltase is composed of duplicated catalytic domains, N- and C-terminal. Each domain displays overlapping specificities. Scientists have discovered the crystal structure for N-terminal human sucrase-isomaltase (ntSI) in apo form to 3.2 Å and in complex with the inhibitor kotalanol to 2.15 Å resolution. [15]