What is a serine hydrolase?
930908
In biochemistry, serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in proteins) that are characterised by the presence of a serine residue in the active site of the enzyme. Serine proteases are grouped into clans that share structural homology and then further subgrouped into families that share close sequence homology. The major clans found in humans include the chymotrypsin-like, the subtilisin-like, the alpha/beta hydrolase, and signal peptidase clans. Serine proteases participate in a wide range of functions in the body, including blood clotting, immunity, and inflammation, as well as contributing to digestive enzymes in both prokaryotes and eukaryotes.
16275
Lipase.\n\n\nlipase (lī'pās) , any enzyme capable of degrading lipid molecules. The bulk of dietary lipids are a class called triacylglycerols and are attacked by lipases to yield simple fatty acids and glycerol, molecules which can permeate the membranes of the stomach and small intestine for use by the body. Gastric lipase, secreted by the stomach lining, has a pH value for optimal activity around neutrality and would appear, therefore, to be essentially inactive in the strongly acid environment of the stomach. It is suggested that this enzyme is more important for infant digestion since the gastric pH in infancy is much less acid than later in life. Most lipid digestion in the adult occurs in the upper loop of the small intestine and is accomplished by a lipase secreted by the pancreas. Phospholipases are the enzymes that degrade phospholipids.
552965
Papain enzyme from papayas and bromolein enzyme from pineapple.
37562
The enzymes in the stomach require a certain pH for the amino acids in them to work properly. So, when the pH is optimum, the amino acids are in their correct ionic state. This enables the enzymes to function properly in digestion.
99518
Certain types of cells attach themselves to, let's say, the walls of a cell culture flask by adhesion molecules, which are specific membrane surface proteins. If you add trypsin, which is a protease (enzyme capable of cleaving proteins), it digests these molecules and causes the cells to detach. Of course, trypsin can digest other cell surface proteins as well, therefore cells might eventualy die if overexpossed to trypsin.
180689
Proteinase K is just going to aid in the extraction of DNA - it basically chews up all of the cellular proteins so that you can isolate the DNA from its cellular material and histones.  For example, if you are extracting DNA from a cheek scraping, you would want to lyse the cells either by boiling them or treating them with a basic solution.  Either of these could contain proteinase K for better cell lysis.  You would then want to neutralize the solution and perform a phenol chloroform extraction to get rid of the chewed up proteins and lipids.
631249
www.enzymes.comClose Window \nTransformation:   TPP™ Protease  (#8)\n\n \n\nHighly Stable and Functional Systemic Enzymes \n\n\n\nImpaired Kidney Function \nHeavy Metal Toxins \nModulation of the Immunce System \n\n\nTPPTM Protease is a proprietary blend of highly active proteolytic enzymes with a wide range of pH stability. Proteolytic enzymes taken orally under certain conditions have been shown to be absorbed in substantial quantities into the blood. Once in the blood circulation, the enzymes in this blend bind to serum proteins, particularly alpha 2-macroglobulin (a2M), and impart immunomodulatory benefits. One of the best-established functions served by the oral proteases in TPPTM blend is in the maintenance of normal blood flow. This is accomplished by breaking down blood clots (fibrinolysis) and platelet aggregation within blood vessels and breaking down excess extra-vascular plasma proteins as in edema. TPPTM Protease will also enhance the hydrolysis of food proteins for enhanced bio-availability of amino acids. \n\n\n\nINDICATIONS: \n\nIMPAIRED KIDNEY FUNCTION - Glomerulonephritis: In this disease there is a build up of protein in the basement membrane of the glomeruli of the kidneys. Fluids must pass through this basement membrane in the initial phase of the filtration of the blood by the kidneys. Recent research using an animal model of this disease "lends further support to the concept that enzymes capable of degrading immune complexes in situ can ameliorate glomerulonephritis". \nHEAVY METAL TOXINS - Heavy metals such as lead (Pb) and mercury (Hg) exert their poisoning effect by binding to ionizable or sulfhydryl groups of proteins, including vital enzymes. Once these metals bind to an essential functional protein, such as an enzyme, they denature and/or inhibit it. This interaction of heavy metals to proteins can lead to degenerating diseases, nerve damage or even death. When taken on an empty stomach, it should be noted that protease is readily taken up into the mucosa cells of the intestine and passed into blood circulation. Clinical observations have noted that upon high intake of TPPTM Protease, heavy metal concentrations have been significantly decreased in the blood. \nMODULATION OF THE IMMUNE SYSTEM - As a result of their coupling to a2M, Tzymeô proteolytic enzymes exhibit an increased binding of several very important cytokines (hormones-like molecules which have a powerful influence on immune cells) such as Transforming growth factor-beta (TGF-b), and Tumor Necrosis Factor-alpha (TNF-a). Studies have indicated that oral hydrolytic enzymes affect cytokine synthesis and modulatory effects. For instance, TNF-a synthesis, which is a necessary step in host defense against tumor cells, is impaired when experimentally inactivated oral proteolytic enzymes were used. Thus, active, GI stable and functional oral enzymes that are absorbed in the blood stream can provide therapeutic applications. In addition, studies have shown that oral proteolytic enzymes increased the tumoricidal and cytotoxic activities of polymorphonuclear neutrophils. COMPONENT BENEFITS: \nTzymeTM Protease Blend in TPPTM Protease provides vital systemic benefits that include support of adequate blood rheology for optimum flow of immune cells, their meditating molecules, hormones, blood cells and other vital molecules and cells. The superb absorption abilities and high functionality of this product are certain to enhance and optimize overall protein hydrolysis. These benefits, in turn, facilitate and support a wide array of metabolic processes. \n\nBromelain, an important addition to the TzymeTM Protease Blend, is a protease derived from the pineapple plant. It has been used for many years as a digestive aid, anti-inflammatory and burn debridement agent. Its actions help to prevent swelling/edema, promote smooth muscle relaxation, inhibit platelet aggregation, and enhance antibiotic absorption. Bromelain is also used in cancer treat
888203
i think its ligase! coz kinase is something thAT SPLITS and ligase is an enzyme tht joins. not sure whether ligase acts agaits kinase
731164
pH: pH is a measure of the acidity or hydrogen ion concentration of a solution. It is measured on a scale of 0-14 with pH values below 7 being acidic, values above 7 being basic and a value around 7 is neutral. As the pH drops into the acidic range an enzyme tends to gain hydrogen ions from the solution. As the pH moves into the basic range the enzyme tends to lose hydrogen ions to the solution. In both cases the changes produced in the chemical bonds of the enzyme molecule result in a change in conformation that decreases enzyme activity.\n\nHope this helps :)
163443
The enzyme catalase is a protein molecule. Its shape, particularly the shape of the active site, is changed by variation of pH from pH7.\nGreater the change away from about pH7, greater the alteration of shape.\nAs the shape of the active site changes the enzyme is less and less effective.\nIncreases or decreases in pH will reach the point where the enzyme's shape is permanently changed - the enzyme is denatured.
877465
Please see Google search on Secreted Alkaline Phosphatase (SEAP). Highly technical- difficult to explain.
735029
The active site of an enzyme is the binding site where catalysis occurs. The structure and chemical properties of the active site allow the recognition and binding of the substrate.\n\nThe active site is usually a small pocket at the surface of the enzyme that contains residues responsible for the susbtrate specificity (charge, hydrophobicity, steric hindrance) and catalytic residues which often act as proton donors or acceptors or are responsible for binding a cofactor such as Pyridoxal, Thiamine or NAD.
353146
It is an enzyme that can counteract the damagging effects of oxygen in tissues. Like the vitamin E.
400539
This has been treated by trypsin and this is the fragment that you would expect.
255214
Proteins are large molecules that are made from amino acids, which are small molecules.
942241
hydrolysis is the breaking apart of polymer such as a carbohydrate, protein, or lipid.
514398
tryptophan a kind of amino acid