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Pepsin is inactive at pH 6.5 and above, however pepsin is not fully denatured or irreversibly inactivated until pH 8.0. [11] [15] Therefore, pepsin in solutions of up to pH 8.0 can be reactivated upon re-acidification. The stability of pepsin at high pH has significant implications on disease attributed to laryngopharyngeal reflux. Pepsin ...
Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...
The enzymes that are secreted in the stomach are gastric enzymes. The stomach plays a major role in digestion, both in a mechanical sense by mixing and crushing the food, and also in an enzymatic sense, by digesting it. The following are enzymes produced by the stomach and their respective function: Pepsin is the main gastric enzyme.
A defect of the enzyme results in the premature breakdown of red blood cells. This destruction of red blood cells is called hemolysis. [6] Red blood cell breakdown may be triggered by infections, certain medication, stress, or foods such as fava beans. [1] [3] Depending on the specific mutation the severity of the condition may vary. [2]
Another term used to describe these disorders is "enzymopathies". This term was created following the study of biodynamic enzymology , a science based on the study of the enzymes and their products. Finally, inborn errors of metabolism were studied for the first time by British physician Archibald Garrod (1857–1936), in 1908.
An exoenzyme, or extracellular enzyme, is an enzyme that is secreted by a cell and functions outside that cell. Exoenzymes are produced by both prokaryotic and eukaryotic cells and have been shown to be a crucial component of many biological processes. Most often these enzymes are involved in the breakdown of larger macromolecules.
The word enzyme was used later to refer to nonliving substances such as pepsin, and the word ferment was used to refer to chemical activity produced by living organisms. [13] Eduard Buchner submitted his first paper on the study of yeast extracts in 1897.
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]