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.
Knox R.B., 1979: Pollen development and quantitative cytochemistry of exine and intine enzymes in sunflower helianthus annuus. Annals Of Botany (london): 95-106 High resolution cytochemical methods were used to characterize pollen development and pollen wall structure in H. annuus. Aniline-blue fluorescent material, presumably callose, was detected in the nexine layer throughout its development. It was [...]
Flanegan J.B., 1982: Poliovirus rna dependent rna polymerase synthesizes full length copies of poliovirion rna cellular messenger rna and several plant virus rna species in vitro. Journal Of Virology: 209-216 The poliovirus Rna-dependent Rna polymerase was active on synthetic homopolymeric Rna templates and on every natural Rna tested. The polymerase copied poly(A).cntdot.oligo(U), poly(C).cntdot.oligo(I), and poly(I).cntdot.oligo(C) [...]
Baltimore D., 1985: Poliovirus replicase stimulation by terminal uridylyl transferase. Journal Of Biological Chemistry2: 7628-7635 In an in vitro poliovirus replication system, purified viral polymerase, plus sence virion Rna, and a host factor were previously shown to be necessary for the transcription of minus strands. It was found that a partially purified eukaryotic initiation factor-2 [...]
Paddon H.B., 1980: Poliovirus increases phosphatidyl choline biosynthesis in hela cells by stimulation of the rate limiting reaction catalyzed by ctp phospho choline cytidylyl transferase. Journal Of Biological Chemistry: 1064-1069 The mechanism by which poliovirus stimulates the incorporation of choline into phosphatidylcholine of HeLa cells was investigated. The uptake of the labeled choline was unchanged [...]
Kovar, J.; Brzobohaty, B.; Studnickova, M., 1982: Polarographic study of zinc bound to alcohol dehydrogenase ec 220.127.116.11. Bioelectrochemistry and Bioenergetics 9(3): 333-344 The differential pulse polarogram of native liver alcohol dehydrogenase consists of 2 peaks which correspond to the reduction of Zn associated with the enzyme. On the basis of its electrochemical properties, peak I [...]
Kovar, J.; Brzobohaty, B.; Studnickova, M., 1982: Polarographic study of zinc binding to glutamate dehydrogenase ec 18.104.22.168. Bioelectrochemistry and Bioenergetics 9(3): 345-356 The interaction of glutamate dehydrogenase with Zn ions was analyzed by d.d. n. The n. of the equimolar enzyme-Zn2+ mixtures consist of a wave with a maximum if scanned using low pulse widths. [...]
Maret W., 1985: Polarographic study of horse liver alcohol dehydrogenase lacking zinc ions at the active sites. Bioelectrochemistry & Bioenergetics6: 407-416 In the differential pulse polarogram of this enzyme only one peak (at the potential of -1.1 V) was detected. The behaviour of this peak under changing polarographic conditions was similar to that of one [...]
Kinoshita H., 1981: Polarographic studies on proteins. Bioelectrochemistry & Bioenergetics: 151-166 Basic information concerning the behavior, on electrochemical reduction and oxidation, of proteins and enzymes at a Hg-electrode and other electrodes is summarized. The electrochemical behavior of ferredoxin at a Hg electrode is interpreted on the basis of the theory of surface redox reaction. Equations [...]
Makinen M.W., 1986: Polarized single crystal absorption spectra of cobalt carboxypeptidase a. Journal Of The American Chemical Society6: 5003-5004 Recent X-ray diffraction studies from this laboratory have shown that the coordination structure of Co2+-reconstituted carboxypeptidase A is essentially identical with that of the native enzyme. The protein donor-ligand atoms are the N.delta./1 atoms of His-69 [...]
Chetty C.S., 1983: Polarization of selected oxidoreductases in the axoplasm of sheep medulla oblongata during electro induced intracellular transport. Indian Journal Of Comparative Animal Physiology: 77-82 Axoplasmic lactate, succinate and malate dehydrogenases as well as cytochrome C oxidase have differential positive charge densities as revealed by the rates of cathodal transport in the sheep medulla [...]