what are the criteria for choosing enzyme inhibitors as a potential drug for therapeutic treatment of disease?
489441
First, it has to inhibit the enzyme you want and not inhibit anything else. It also has to not cause any undesired effects by inhibiting the target enzyme. Sometimes the same enzyme is present in more than one tissue, so the same inhibitor can fix a problem in one organ and cause a problem somewhere else.\n\nNext the drug needs to be soluble. As you digest a pill, receive a shot, or take an IV, the drug becomes diluted as it enters the bloodstream. If it isn't very soluble to begin with, it's nearly impossible to reach therapeutic concentrations in a patient.\n\nThe drug also must be able to reach it's target. If the target enzyme exists inside a cell, the drug must be able to enter the cell. Often a great inhibitor makes a lousy drug because it can get through the plasma membrane.\n\nFinally the drug should ideally be left alone by the Cytochrome P450 enzymes of the liver. Many drugs are metabolized by P450, which is why this is a major source of drug interactions. Further, some of the P450 isotypes vary widely from person to person. This means that the safe dose for one person could be lethal in another, and at this point it's basically impossible to predict who those people are.\n\nThe bottom line is that the drug has to be bioavailable, safe and effective.
317821
(m)\n\nmetabolic pathway analysis, it should be considered that many enzymes operate with low specificity (e.g. nucleoside diphosphokinase, uridine kinase, transketolase, aldolase), so that various substrates and products can be converted. Here, we analyze the effect of enzymes with low substrate specificity on the elementary flux modes (pathways). We also study the benefits of two different approaches to describing multifunctional enzymes. The usual description is in terms of (overall) enzymatic reactions. At a more detailed level, the reaction steps (half-reactions, hemi-reactions) of the formation and conversion of enzyme-substrate complexes are considered. Multifunctional enzymes operate according to various mechanisms. This is illustrated here by the reaction schemes for the different enzyme mechanisms of bifunctional enzymes. For enzymes with two or more functions, it is important to consider only linearly independent functions, because otherwise cyclic elementary modes would occur which do not perform any net transformation. However, the choice of linearly independent functions is not a priori unique. We give a method for making this choice unique by considering the extreme pathways of the hemi-reactions system. A formal application of the algorithm for computing elementary flux modes (pathways) yields the result that the number of such modes sometimes depend on the level of description if some reactions are reversible and the products of the multifunctional enzymes are external metabolites or some multifunctional enzymes partly share the same metabolites. However, this problem can be solved by appropriate interpretation of the definition of elementary modes and the correct choice of independent functions of multifunctional enzymes. The analysis is illustrated by a biochemical example taken from nucleotide metabolism, comparing the two ways of description for nucleoside diphosphokinase and adenylate kinase, and by several smaller examples.
321826
Usually, new drugs are developed through methods involving a test tube and isolated proteins and/or DNA. Would you like to be the first to try a new drug? It can be very dangerous.\n\nIn order to try to maximize safety from side effects, we test these drugs on human and/or animal cells in culture, then with animal models to see if there are potentially serious side effects we don't expect. Phase III clinical trials finally test the drugs in limited doses on human subjects.
692497
It is an enzyme, all enzymes have specific targets due to protein makeup of the molecule. This enzyme is secreted to disolve clots which inhibit the spread of strep in the body.
170878
Since this would involve subjecting a living cell or organism to the effects of the drug...and let's say that we are talking about a human;\nfactors include how fast and thorough the drug would go through the organism, how fast and thorough the drug would exit the organism, side effects of the drug, the actual physical makeup of the organism, administration method, medical background of the organism, what other drugs and nutrients are present in the organism, if the organism is active or not during administration...I'm sure I could go on!
1170912
enzyme unit (U or EU) \na unit used by biochemists to measure the activity of enzymes, which are proteins produced by living cells to cause or facilitate necessary chemical reactions within the cell. One enzyme unit is the quantity of enzyme needed to cause a reaction to process 1 micromole of substance per minute under specified conditions. Thus, one enzyme unit has a catalytic activity of 1/60 microkatal (µkt) or 16.667 nanokatals (nkt). \n\n \n\ninternational unit (IU) \na unit used to measure the activity (that is, the effect) of many vitamins and drugs. For each substance to which this unit applies, there is an international agreement specifying the biological effect expected with a dose of 1 IU. Other quantities of the substance are then expressed as multiples of this standard. Examples: 1 IU represents 45.5 micrograms of a standard preparation of insulin or 0.6 microgram of a standard preparation of penicillin. Consumers most often see IU's on the labels of vitamin packages: in standard preparations the equivalent of 1 IU is 0.3 microgram (0.0003 mg) for vitamin A, 50 micrograms (0.05 mg) for vitamin C, 25 nanograms (0.000 025 mg) for vitamin D, and 2/3 milligram for (natural) vitamin E. Please note: for many substances there is no definite conversion between international units and mass units (such as milligrams). This is because preparations of those substances vary in activity, so that the effect per milligram of one preparation is different from that of another.
407058
Drugs - anti inflammatory
905117
full information leaflet available here\n\nhttp://www.patient.co.uk/showdoc/27000881/
1054558
no works as competitive inhibitors to inhibit the bacteria enzyme
830201
Look at one of these sites, and contact persons listes on them:\nhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16935061&dopt=Abstract\nhttp://www.amedeo.com/medicine/reh/arpmre.htm\nhttp://bjsm.bmj.com/cgi/content/full/39/6/373\nhttp://bjsm.bmj.com/cgi/reprint/39/6/373.pdf
279794
figure out the efgfect of the enzyme. Or you can test DNA structure. Inhibitary enzymes have a blacked actionsite whereas activation enzymes have activation sites open to substrates
498975
An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. The word comes from the Greek ένζυμο, énsymo, which comes from én ("at" or "in") and simo ("leaven" or "yeast"). Certain RNAs also have catalytic activity, but to differentiate them from protein enzymes, they are referred to as RNA enzymes or ribozymes.\n\nEnzymes are essential to sustain life because most chemical reactions in biological cells would occur too slowly, or would lead to different products without enzymes. A malfunction (mutation, overproduction, underproduction or deletion) of a single critical enzyme can lead to a severe disease. For example, the most common type of phenylketonuria is caused by a single amino acid mutation in the enzyme phenylalanine hydroxylase, which catalyzes the first step in the degradation of phenylalanine. The resulting build-up of phenylalanine and related products can lead to mental retardation if the disease is untreated.\n\nLike all catalysts, enzymes work by providing an alternate pathway of lower activation energy of a reaction, thus allowing the reaction to proceed much faster. Enzymes may speed up reactions by a factor of many millions. An enzyme, like any catalyst, remains unaltered by the completed reaction and can therefore continue to function. Because enzymes do not affect the relative energy between the products and reagents, they do not affect equilibrium of a reaction. However, the advantage of enzymes compared to most other catalysts is their sterio-, regio- and chemoselectivity and specificity.\n\nEnzyme activity can be affected by other molecules. Inhibitors are naturally occurring or synthetic molecules that decrease or abolish enzyme activity; activators are molecules that increase activity. Some irreversible inhibitors bind enzymes very tightly, effectively inactivating them. Many drugs and poisons act by inhibiting enzymes. Aspirin inhibits the COX-1 and COX-2 enzymes that produce the inflammation messenger prostaglandin, thus suppressing pain and inflammation. The poison cyanide inhibits cytochrome c oxidase, which effectively blocks cellular respiration.\n\nWhile all enzymes have a biological role, some enzymes are used commercially for other purposes. Many household cleaners use enzymes to speed up chemical reactions ( e.g., breaking down protein or starch stains in clothes).\n\nMore than 5,000 enzymes are known. Typically the suffix -ase is added to the name of the substrate (e.g., lactase is the enzyme that catalyzes the cleavage of lactose) or the type of reaction (e.g., DNA polymerase catalyzes the formation of DNA polymers). However, this is not always the case, especially when enzymes modify multiple substrates. For this reason Enzyme Commission or EC numbers are used to classify enzymes based on the reactions they catalyze. Even this is not a perfect solution, as enzymes from different species or even very similar enzymes in the same species may have identical EC numbers.\nIn enzymes, as with other proteins, function is determined by structure. An enzyme can be:\n\n    * A monomeric protein, i.e., containing only one polypeptide chain, typically one hundred or more amino acids; or\n    * an oligomeric protein consisting of several polypeptide chains, different or identical, that act together as a unit.\n\nAs with any protein, each monomer is actually produced as a long, linear chain of amino acids, which folds in a particular fashion to produce a three-dimensional product. Individual monomers may then combine via non-covalent interactions to form a multimeric protein. Many enzymes can be unfolded or inactivated by heating, which destroys the three-dimensional structure of the protein.\n\nhttp://en.wikipedia.org/wiki/Enzyme#3D_Structure
1029974
More info is necessary.\nHow were the enzymes prepared and purified?\nWhat's your exact experiment?\nDo you see an increase in enzyme activity when you put both Ca and EDTA at the same time and if so at which molar ratio of the two effectors?\nDo you also see activation for each effector separately? How does it compare quantitatively to the effect of the combination of the effectors?\n\nMy wild guess would be that Ca+2 is an allosteric activator, EDTA removes another metal that was co-purified with the enzyme and the latter metal is an inhibitor. If  both have a positive effect on their own and an even higher when combined then it could be the case.\nAnother more extreme case is that EDTA removes the catalytic ion (if it can form a more stable complex than with Ca) and Ca takes its place. Then EDTA alone should kill the reaction while in combination with Ca have a positive effect. However this is a quite improbable scenario since enzymes usually have evolved for best performance and thus the enzyme would be expected to have the very common Ca+2 in the catalytic center to begin with, if Ca+2 aids the reaction more.
539469
Enzymatic activity can be quantatively define, but it is very specific, depend on what kind of emzyme reaction and what experimental approach to access it.
234224
Time being we cant find the cure but there are ways of slowing down the process and lessen the inflammation..usage of steroids help in reducing the damage....the main reason we cant find the cure is because we cant find the main cause of this particular disease...\nMultiple sclerosis (MS) is an inflammatory, demyelinating disease of the central nervous system (CNS). MS lesions, characterized by perivascular infiltration of monocytes and lymphocytes, appear as indurated areas in pathologic specimens; hence, the term "sclerosis in plaques." \n\nPrevent relapses or disease progression by using the “ABCR” immunomodulatory drugs (ie, interferon beta-1a IM [Avonex], interferon beta-1b SC [Betaseron], glatiramer acetate SC [Copaxone], or interferon beta-1a SC [Rebif]). These 4 medications have been approved by the US FDA and are currently used in the United States as first-line therapies for MS. As a rule of thumb, the ABCR medications tend to decrease the rate of MS relapses by approximately one third, with the highest efficacy demonstrated in clinical trials for the high-dose, high-frequency interferons (ie, Betaseron [34%] and Rebif [33%]).\n\nbut still there is no cure..only drugs to prevent the progression...
2805
Wow... that's a question that could be answered on many different levels, and you're optimistic as hell to think you can get a "real" answer here. Basically, an enzyme provides a micro-enviroment that is very conducive to the formation of an intermediate form that leads from the substrate to the product. Another way of saying this is that an enzyme, like any other catalyst, lowers the activation energy of a reaction.\n\nBut seriously, dude. You're asking for a course in biochemistry here. Try Stryer, or any other classic biochem textbook, for a more thorough answer.
519670
remicade is an intravenous medication.  It is used for arthritis and sometimes for crohn's disease.