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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.

Preliminary evaluation of cocarboxylase in protecting the ischemic myocardium

Anon, 1988: Preliminary evaluation of cocarboxylase in protecting the ischemic myocardium. Compendium De Investigaciones Clinicas Latinoamericanas: 74-80 Cocarboxylase (Cc), also known as thiamin pyrophosphate, is an important coenzyme for pyruvate dehydrogenase. Pyruvate dehydrogenase is the regulating enzyme for pyruvate catabolism and a possible key enzyme involving recovery of the ischemic myocardium. A stable solution of [...]


Preliminary data on the genetic differentiation of onchocerca volvulus in africa nematoda filarioidea

Bullini L., 1985: Preliminary data on the genetic differentiation of onchocerca volvulus in africa nematoda filarioidea. Acta Tropica: 341-352 Data are reported on the genetic structure of three Onchocerca volvulus populations, respectively from Mali (savanna), Ivory Coast (forest), and Zaire (forest gallery in savanna). Electrophoretic analysis, carried out on 25 gene-enzyme systems, has shown a [...]


Preliminary crystallographic study of omega amino acid pyruvate amino transferase ec 2.6.1.55 from pseudomonas sp f 126

Morita, Y.; Aibara, S.; Yonaha, K.; Toyama, S.; Soda, K., 1979: Preliminary crystallographic study of omega amino acid pyruvate amino transferase ec 2.6.1.55 from pseudomonas sp f 126. Journal of Molecular Biology 130(2): 211-213 Large single crystals of.omega.-amino acid:pyruvate aminotransferase, were prepared by dialysis of the enzyme solution against 2.2 M-(Nh4)2so4 solution at pH 7. [...]


Preliminary crystallographic studies on the coenzyme binding to glyceraldehyde 3 phosphate dehydrogenase from palinurus versicolor

Zou C., 1988: Preliminary crystallographic studies on the coenzyme binding to glyceraldehyde 3 phosphate dehydrogenase from palinurus versicolor. Scientia Sinica Series B (chemical Biological Agricultural Medical & Earth Sciences): 313-318 The three forms of glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor muscle, namely apo native enzyme, apo carboxymethylated enzyme and the enzyme carrying two fluorescent Nad derivatives [...]


Preliminary characterization of phenyl oxidase activity in the salivary secretion of the parasite exeristes roborator

Thompson S.N., 1980: Preliminary characterization of phenyl oxidase activity in the salivary secretion of the parasite exeristes roborator. Journal Of Insect Physiology: 505-510 Melanization of artificial media which was due to phenyloxidase activity secreted by the developing larvae into the diet accompanied feeding by the parasite E. roborator. The enzyme was localized in the salivary [...]


Preliminary characterization of laminarinase from trichoderma longibrachiatum

Nakas J.P., 1987: Preliminary characterization of laminarinase from trichoderma longibrachiatum. Enzyme & Microbial Technology: 89-93 Trichoderma longibrachiatum, when cultured on untreated ground mushroom (Agaricus bisporus) fruiting bodies as the only carbon substrate, exhibited extracellular laminarinase (endo-1,3(4)-.beta.-glucanase Ec 3.2.1.6) activity. The general physicochemical and catalytic properties of that enzyme preparation were examined. The apparent Km and [...]


Preliminary characterization of adenosine deaminase ec 3.5.4.4 from bacillus cereus

Sgarrella, F.; Mura, U.; Catalani, R.; Pitti, A.; Ipata, P. L., 1982: Preliminary characterization of adenosine deaminase ec 3.5.4.4 from bacillus cereus. Bollettino Societa Italiana Biologia Sperimentale 58(18): 1145-1151 Adenosine deaminase (Ec 3.5.4.4) from B. cereus is quite unstable, like other bacterial deaminases, but some monovalent cations have an unusual stabilizing effect on the enzyme. [...]


Preliminary characterization of a chinese hamster ovary cell glycosylation mutant isolated by screening for low intracellular lysosomal enzyme activity

Krag S.S., 1986: Preliminary characterization of a chinese hamster ovary cell glycosylation mutant isolated by screening for low intracellular lysosomal enzyme activity. Molecular & Cellular Biochemistry2: 35-46 A novel screening procedure was developed for isolating Chinese hamster ovary cell mutants altered in the early steps of the biosynthesis of asparagine-linked glycoproteins. This procedure identifies cells [...]


Preliminary characterization of a cholin esterase from roots of bengal gram cicer arietinum

Maheshwari S.C., 1980: Preliminary characterization of a cholin esterase from roots of bengal gram cicer arietinum. Plant & Cell Physiology: 1675-1680 A cholinesterase was isolated and purified (65-fold) from roots of Bengal gram (C. arietinum L.) seedlings. It hydrolyzes acetylcholine and acetylthiocholine more readily than propionylthiocholine or butyrylthiocholine. The enzyme has high affinity for acetylthiocholine [...]


Preliminary characterization and physical properties of pyridoxal oxidase activity from drosophila melanogaster

Hanly E.W., 1980: Preliminary characterization and physical properties of pyridoxal oxidase activity from drosophila melanogaster. Molecular & General Genetics: 455-462 A method of extracting pyridoxal oxidase (Po) activity from D. melanogaster adults is described. In crude extracts, this method allows the activity to remain stable for an extended period of time so that subsequent work [...]