The word “enzyme” is derived from the Modern Greek “enzumos,” which directly translates into “leavened.” Enzymes are generally biological molecules that living organisms produce in order to catalyze (which, in this case, to increase the speed or rates of) specific biochemical reactions. The substrates, which are what molecules are called at the beginning of the enzymatic reaction, will be converted into different molecules, known as products. Almost every chemical reaction that occurs in a biological cell will need enzymes in order to perform at a rate that is sufficient for sustaining life.
As with other biological catalysts, enzymes function through the process of lowering the activation energy for a reaction. This process will dramatically increase the rate of the enzymatic reaction and will allow the products (the result of enzymatic reactions) to form faster, and for reactions to achieve their equilibrium states in a shorter amount of time. With the use of enzymes as catalysts, the reactions are a million times faster than those reactions that do not utilize enzymes.
The activity of enzymes can be affected by other molecules. Inhibitors are known to be molecules that decrease the activity of enzymes, while activators are known as molecules that increase the activity of enzymes. Many kinds of drugs and poisons function as enzyme inhibitors. The activity of enzymes can also be affected by pressure, temperature, the chemical environment, and the concentration of a specific substrate.
There are enzymes that are used for commercial purposes, such as in the synthesis of various antibiotics. Some household products use enzymes in order to speed up several biochemical reactions—enzymes are known to be used in biological washing powders that are designed to break down protein and fat stains on clothes.
This category contains scientific information on enzymes, which are biological molecules that living organisms produce in order to catalyze (which, in this case, to increase the speed or rates of) specific biochemical reactions.
Rothman S.S., 1982: Food duodenal extracts and enzyme secretion by the pancreas. American Journal Of Physiology: G304-G312 Previous studies have reported that injection of duodenal extracts from rats fed different meals into the celiac artery of recipient rats elicited the secretion of related pancreatic enzymes. This laboratory was unable to reproduce the enzyme-specific increases in [...]
Boutin B.K., 1983: Food borne entero toxigenic escherichia coli detection and enumeration by dna colony hybridization. Applied & Environmental Microbiology: 1324-1330 Four methods were compared for detecting heat-labile toxin production by E. coli: Dna colony hybridization, 2 enzyme-linked immunosorbent assays and the mouse Y-1 adrenal cell reaction. Although results of the methods were in general [...]
Yoshida H., 1984: Food allergy in atopic dermatitis measurement of allergen specific immunoglobulin e and immunoglobulin g 4 antibodies by using radioallergosorbent test and enzyme linked immunosorbent assay elisa. Hifu: 611-616 Allergen-specific IgE and IgG4 antibodies against 13 food allergen extracts (wheat, rice, corn, buckwheat, peanut, egg white, cow’s milk, pork, codfish, tunny, salmon, crab [...]
Ferone R., 1985: Folylpoly gamma glutamate synthetase dihydrofolate synthetase cloning and high expression of the escherichia coli fol c gene and purification and properties of the gene product. Journal Of Biological Chemistry: 5625-5630 The E. coli gene for folylpolyglutamate synthetase-dihydrofolate synthetase was localized to plasmids pLC22-45, 24-31 and 28-44 of the Clarke-Carbon E. coli colony [...]
Shane B., 1981: Folyl poly gamma glutamate synthesis by bacteria and mammalian cells. Molecular & Cellular Biochemistryrt 2: 209-228 The purification and properties of folylpolyglutamate synthetase from Corynebacterium and some properties of partially purified enzyme from Lactobacillus casei, Streptococcus faecalis, Neurospora crassa, pig liver, and Chinese hamster ovary cells, are described. The Corynebacterium enzyme catalyzes [...]
Nagashima H., 1981: Follow up study in chronic active hepatitis after therapies with immuno suppressive drugs and tiopronin. Gastroenterologia Japonica: 568-575 Follow-up studies were conducted in patients with chronic active hepatitis treated 10 yr ago with tiopronin (Tp) or corticosteroids (Cs). Hepatitis B surface antigen (HBsAg) was measured in previously collected paraffin embedded liver sections [...]
Kertai P., 1986: Follow up of settlement and mitosis of leukemic lymphoblasts by enzyme activity determination in akr and hss inbred mice the effect of genetic factors. Magyar Onkologia: 32-37 The authors transplanted lymphoid leukaemic cells of Akr and Hss origin into Akr and Hss.times. Akr/F1 mice and studied the changes of pyruvate kinase activity [...]
Tovey L.A.D., 1985: Follow up of normal individuals with a positive antiglobulin test. Scandinavian Journal Of Haematology: 348-353 Over a period of 20 yr (1962-1982), 67 apparently fit donors at a Regional Blood Transfusion Service were found to have an unexplained positive direct antiglobulin test (Dat). During 1983, 26 were traced and re-tested. 9 still [...]
Netzloff M.L., 1986: Follow up of language and cognitive development in patients with mannosidosis. Archives Of Neurology: 157-159 Three brothers with mannosidosis were assessed both biochemically by levels of enzyme activities and developmentally by serial testing of language and cognitive development. The findings indicated that while the leukocyte enzyme activity of.alpha.-mannosidase was exceptionally low, only [...]
Hamaya K., 1980: Follow up 10 years after cortico steroid therapy for chronic active hepatitis type b. Hepato Gastroenterology: 85-90 Follow-up studies were conducted on chronic liver disease patients treated 10 yr previously with corticosteroid (Cs). Hbs antigen (HbsAg, hepatitis type B surface antigen) was measured in previously collected paraffin embedded liver sections by enzyme-labeled [...]