Properties of Enzyme Catalysts

Properties of Enzyme Catalysts Introduction Enzymes:Enzymes are single or multiple -chain proteins that act as a biological catalysts with the ability to promote specific chemical rxn under the mild condition that prevail in most living organism. Over-view of Enzymes catalysts All reaction in the body are mediated by enzymes, which are protein catalysis that increase the rate of reaction without being changed in overall process. Among the many biologic reaction that are energetic possible, Enzyme selectively channel reactant called substrate into useful pathways. Enzynes thus direct all metabolic events. Enzyme are Protein Catalyst that increase the velocity of the chemical rxn, and are not consumed during the rxn they catalyse. Some type of RNA act like a Enzyme, RNA with catalytic activity are called Ribozymes. Enzymes are protein catalysts, they influence the kinetics but not the thermodynamics of a reaction Increase the rate of a chemical reaction Do not alter the equilibrium Properties of enzymes Enzyme molecules contain a special pocket called a active site. The active site contain amino acid side chain that create a three dimention surface complementary to the substrate . the active site bind the substrate , forming an enzyme substrate (ES) complex. The ES is converted to enzyme product(EP), which subsequently dissociated to enzyme and product. Catalytic efficiency: Most enzyme catalytic rxn are highly efficient , proceeding from 103 to 108 times faster than the uncatalysed rxn. Eacg enzyme molecule is capable of transforming 100 to 1000 substrate molecules into product each sec. The number of molecules of substrate converted to product is called the turnover no. Characterstic of Enzymes Certain substance is small amount have unique capacity of speedingup chemical rxn without being alter after the rxn, they acceleration the velocity of the rxn without necessary initially it. Substance that behave in this manner are called catalyst or catalytic agent. For eg hydrogen and oxygen do not combine to any appreciable extent under normal atmospheric condition. However unlike platinum , while is inorganic , enzyme are organic compound produce by living organism. Thus we may define enzyme as organic catalyst produced by a organic cell. The three distinctive characterstic are 1)specificity. 2)high Catalyst rate 3)high capacity for regulation. A general model of reaction kinetics of biological systems Dyanamic mathematical model in biotechnology require beside the information require the stoiciometry ok the biological rxn system.. The identification of a priori unknown reaction kinetics is often a critical task due to the non-linearity and (over-) parameterization of the model equations introduced to account for all the possible modulation phenomena. The contribution of this paper is to propose a general formulation of reaction kinetics, as an extension of the Michaelis-Menten kinetics, which allows limitation/activation and inhibition effects to be described with a reduced number of parameters. The dianamic model of a perfectly stirred tank bioreactor is usually derived from a mass balance which lead to a differential eq systwm for the concentration vector ) = c0; r(c(t))=q(c(t))cx0(t) The matrix âÅ'ˆâ‚ ¬R^m*n contains the information on the stoichiometry of the reaction system and is usually timeinvariant. The biological reactions r â‚ ¬ R ^ m are catalysed by the viable biomass, whose concentration is denoted by cx0(t); and the specific reaction rate vector q â‚ ¬R^m is usually a non-linear function of the concentrations. Dâ‚ ¬ R is the renewal (or dilution) rate and u â‚ ¬ R^ n containsthe reactor input/output conditions. There are a large variety of mathematical descriptions of the reaction kinetics available in the literature. A systematic approach is, therefore, necessary to find the best model structure and the best values ofthe model parameters with respect to some imposed criterion. For instance, in terms of model identification, the optimal structure is characterised by minimal correlations between parameters and maximal identifiability properties. In terms of state estimation and control, however, simplicity and (non-)linearity play impo rtant roles.[5] ENZYME CATALYST Most of the rxn that occur in living organism are catalyst by molecule called enzyme. Most enzymes are proteins (certain RNA molecules also act as enzyme). An enzyme is in specific in its action. Many enzymes catalyst only the conversion of a particular reactant to a particular product ;other enzyme catalyst only a certain class of rxn(by ester hydrolysis) . Enzyme speed up rxn rate very substantionally and in their absent most biological rxn occur . The molecule an enzyme act on is called the substrate.the substrate bind to a specific active site on the enzymeso form as enzyme substrate complex. Some physiological poison act by binding to active site of an enzyme,there blocking the action of the enzyme.the structure of an inhibitor may resemble the structure of enzyme substrate .Cyanide act by blocking the enzyme cytochrome oxidase. The single called Escherichia coli, a bacterium that flourished in human colons, contain about 2500 different enzymes .[6] Enzyme Kinetics 1 Michaelis-Menten Kinetics 2.Lineweaver-Burk Kinetics 3. Hanes-Woolf Kinetics 4. Eadie-hofstee 5. Reversible Inhibition[7] K1 k2 E+S ↔ ES ↔ E+P k-1 k-2 E is the free enzyme , S is the substrate, ES is the enzyme substrate complex p is the product. Thp overall rxn is s gives p. The enzyme is assumed in step 1 and rearranged in step 2.Enzymes can catalyze up to several million reactions per second 2.Enzyme rates depend on solution conditions and substrate concentration. Conditions that denature the protein abolish enzyme activity, such as high temperatures, extremes of pH or high salt concentrations, while raising substrate concentration tends to increase activity. To find the maximum speed of an enzymatic reaction, the substrate concentration is increased until a constant rate of product formation is seen. This is shown in the saturation curve on the right. Saturation happens because, as substrate concentration increases, more and more of the free enzyme is converted into the substrate-bound ES form. At the maximum velocity (Vmax) of the enzyme, all the enzyme active sites are bound to substrate, and the amount of ES complex is the same as the total amount of enzyme. However, Vmax is only one kinetic constant of enzymes. The amount of substrate needed to achieve a given rate of reaction is also important. This is given by the Michaelis-Menten constant (Km), which is the substrate concentration required for an enzyme to reach one-half its maximum velocity. Each enzyme has a characteristic Km for a given substrate, and this can show how tight the binding of the substrate is to the enzyme In most experimental studies on enzymes kinetics, the enzyme concentrationis much less than the substrate concentration; [E] [ES]-[E][P] 0=([E] -[E][S])(k[E][S]-[P])-(+)[ES] If [is the initial enzyme concentration than [E]=[E]+[ES].since the conc is [E]during the rxn is generally not known while [E] is known , we replace [E] by [E] The const rate is =- R=[E][S]-[ES] R=[E][S]-([S]+[ES] Since the concentration of the intermediate ES is very small, we have Usually,the rxn is followed only to a few percent completion and the initial rate determined. Setting the product concentration [P]equal to 0 and [S]equal to [S] We get as the initial rate r where the Michaelis Menten const is defined by . The reciprocal of above eq is 1/r= 1/ Equation 2 is the Michaelis Menten eq , and above eq is the Lineweaver Burk eq. One measure r for several [S] values with [E] held fixed. The constant Since [E] is known . strictly speaking r is not the rate at t=0 , since there is a short induction period before steady state condition are establish . Although many exp studies on enzyme kinetic give a rate law in agreement with the Michaelis Menten eq .the mech ‘a is grossly over simplified. For one thing , there is much evidence that , while the substrate is bound to the enzyme , it generally undergoes a chemical change before being released as product . hence a better model is E + S ES ↔ EP ↔ E+ P The above model gives a rate law that has the same form as the Michaelis Menten eq but the const are replaced const with diff significance . Enzyme rxn are quite fast but can be studied using â€Å"classical† methods by keeping [E] and [S]very slow. Lineweaver- Burk Equation The method describe for the determination of is someone complex and therefore simpler method have been devised. Two such method are given below: First method-a convient means of evaluating and is to plot kinetic data as the reciprocals of v and (S) where v velocity and (S) is the total conc of substrate. such a double reciprocal was proposed by Hans Lineweaver and Dean Burk in 1934. If one take the reciprocal of Michaelis Menten eq, the following eq is formed This is known as Lineweaver- Burk Equation. This eq is the form y=mx+b, if one condition the variable to b and 1/(s). When one plots a graph against these two variable , a straight line is obtained . the slop of this line corresponds to and the 1/v intercept corresponds to 1/. Since can be determine from the intercept , the can be calculated . Second method: another graphical method for the measurement of for experimentel data on V as a measure of (S) makes use of the above Lineweaver- Burk Equation . multiplication on sides of the by (S) gives: A plot of verses (S) gives a straight line on axis is and the slope is and can be obtained from intercepy of the slope. A lineweaver burk plots provide a quick test for adhereance to Michaelis Menten eq kinetic and allows easily evaluation of the critical const . it also allow the discrimination between diff kinds of enzyme inhibition and regulation. A disadventure of lineweaver-Burk plot is that a long extrapolation is often require to determine , which corresponds uncertainty in the result. Consequently , other way of plotting the data are sometimes used. Alternate plot are based on Hanes-eq: [s]/v So that v/[s] is plotted against v. The relative merit of the Lineweaver-Burk, Hanes and Edlie-Hoffstee eq for the determination of and are llustrated below in fig. Using the same set of e ixperimental values of v for a series of substrate concentration . it can be seen that the lineweaver-Burk eq gives the unequal distribution of points and greater emphasis to the points at low substrate concentration that are subject to a greater experimental error, whilst the Edlie-Hoffstee eq and a Hans eq gives a better distribution of points. In the case of the Hans plot , greater emphasis is placed on the experimental data at higher substrate 1)Lineweaver plot 2)Hanes plot 3) Eadie-hofstee plot Lineweaver burk, Hanes and Eadie hofstee plot the same set of experimental data of the effect of substrate conc. [S] on the initial rate v of the enzyme catalyst rxn. Reversible Inhibition Now consider the effect of reversibly-binding inhibitors on an enzyme. If an inhibitor binds reversibly at the same site as the substrate, the inhibition is referred to as competitive. If the inhibitor binds to another site on the enzyme, the binding is described as noncompetitive. These two alternative behaviors may be distinguished by their effects on Lineweaver-Burk or Hanes-Woolf plots. If a reversible inhibitor can bind to the enzyme active site in place of the substrate, it is described as a competitive inhibitor. In pure competitive inhibition, the inhibitor is assumed to bind to the free enzyme but not to the enzyme-substrate (ES) complex. The binding is described as shown below: Here Ki is the dissociation constant for the EI complex. EI does not react to form E + P, and the enzyme is unable to bind both S and I at the same time. There are several graphical methods for detecting and analyzing competitive inhibition. The Michaelis-Menten, Lineweaver-Burk, and Hanes-Woolf equations can all be modified to include a term that describes the inhibition by I. Choose one of the cases below to consider each of these in more detail: The Michaelis-Menten equation for competitive inhibition is: The Lineweaver-Burk equation for competitive inhibition is: The Hanes-Woolf equation for competitive inhibition is: Noncompetitive Inhibition If a reversible inhibitor can bind to the enzyme at a site that is distinct from the active site, it is described as a noncompetitive inhibitor. In pure noncompetitive inhibition, the inhibitor binds with equal affinity to the free enzyme and to the enzyme-substrate (ES) complex. The binding is described as shown below: Here Ki is the dissociation constant for either the EI complex or the IES complex. Neither of these complexes can react to form E + P. There are several graphical methods for detecting and analyzing noncompetitive inhibition. The Michaelis-Menten, Lineweaver-Burk, and Hanes-Woolf equations can all be modified to include a term that describes the inhibition by I. Choose one of the cases below to consider each of these in more detail: The Michaelis-Menten equation for noncompetitive inhibition is: The Lineweaver-Burk equation for noncompetitive inhibition is: The Hanes-Woolf equation for noncompetitive inhibition is: Limiting Kinetics of Enzyme-Catalysed Reactions At very low concentrations of substrate many enzyme-catalysed reactions display approximately second-order kinetics, with rate given by the following equation: v = kA [E]0 [A] . . . . . . . in which the symbol kA (or, in general, kR for a reactant R) is the apparent second-order rate constant or specificity constant and [E]0, which may also be written as [E]t or [E]stoich, is the total or stoichiometric concentration of catalytic centres. The rationale for the subscript 0 is that the total enzyme concentration is normally the concentration at the instant of mixing, i.e. at time zero. Conversely, at very high substrate concentrations the same reactions commonly display approximately first-order kinetics (zero-order with respect to substrate): v = k0 [E]0 . in which k0, which may also be written as kcat is the apparent first-order rate constant. Although these limiting types of behaviour are not universally observed, they are more common than Michaelis-Menten kinetics)and provide a basis for classifying inhibitory and other effects independently of the need for Michaelis-Menten kinetics. The quantity k0[E]0 is given the symbol V and the name limiting rate. It is particularly useful when k0 cannot be calculated because the total catalytic-centre concentration is unknown, as in studies of enzymes of unknown purity, sub-unit structure and molecular mass. The symbol Vmax and the names maximum rate and maximum velocity are also in widespread use although under normal circumstances there is no finite substrate concentration at which v = V and hence no maximum in the mathematical sense. The form Vmax is convenient in speech as it avoids the need for a cumbersome distinction between capital V and lower case v. When a true maximum does occur the symbol vmax (not Vmax) and the name maximum rate may be used for the true maximum value of v but care should be taken to avoid confusion with the limiting rate. Enzyme Mechanism: Enzyme kinetic studies,together with the other typeof investigation have led to inside into the way in which enzyme exert their catalytic action.aspects of this are of special interest . This specificityof enzymes is explained in terms of the an elaborating of Fischers â€Å"lock and key†which is concerned with the way in which an enzyme and the substrate fixed together in forming a Enzyme substrate complex and in undergo subsequent rxn . the second aspect is the very high effectiveness of enzyme in comparison with other catalyst. the high effectiveness of catalyst almost always is associate with a low energy of activation for the rxn. in some cases the effect has been attributed to the fact that the enzyme is acting as a bifunctional catalyst, in tha two catalytic group are presentside by side at the active centre. Transition state : When a chemical reaction occurs, the energy content of the reacting molecule or atom increases. This is why most chemical reactions, whether they release heat or absorb heat, happen faster as the temperature is raised. The high-energy state of the reactants is called the transition state. For example, in a bond-breaking reaction, the transition state may be one where the reacting bond, although not completely broken, is vibrating at a frequency high enough that it is equally likely to split apart as to reform. Forming reactants or products results in the loss of energy from the transition state. This principle is shown in Figure 1 , where the increased energy of the transition state is represented as a hill or barrier on the energy diagram. Catalysts reduce the height of the barrier for achieving the transition state. General Catalytic Mechanism Catalysed reaction occur by a wide variety of mechanism.There is however one pattern that applies to a no of single substrate rxns catalysted by surfaces,enzymes, acids and bases. It is useful to consider this schmene of rxn first show as to appreciate the similarities that exist between certain rxn that are catalysted by different type od catalyst. The rxn schme: C + S ↔ X + Y X + W ↔ P + Z Here C represent the catalyst and s is the substrate; X and Y are intermediate , the first of which undergoes a second rxn with a species W to give final product or products P together with the addition substance Z. This scheme shows only the kinetically significance reactions; the substate Y and Z undergo other process that do not have any effect on yhe kinetic behaviour. To simplify the treatment it is assumed that the second rxn does not in the reverse direction ; this can b ensured if the product P is removed as far as it is formed. In surface catalysis X is an adsoption complex, Y and W are non exitance. The const in this case are first order rate const, while is the second order const. In catalysis by acid and base however Y and W play important role. Thus i c is an acid catalyst, rxn 1 involces the transfer of a proton to S,so that Y is the base conjugate to the acid C. In acid catalyst the intermediate X is the protonated substrete SH+ and a rxn 2 is proton is transferred to a species W. The species W therefore has basic properties and it may b molecule of a solvent and a solute. For eg It may be the species Y formed in 1 step . we will see that the kinetic behaviour depends in an important way on wheather the intermediate X transfers its proton to solvent molecule or to a solute molecule. Conversely in base catalyst Y is the acid conjugate to the base C.the intermediate X is the substrate Molecule minus a proton., and in rxn 2 it accepts a proton from W.again we have a solvent molecule or a solute molecule.in some situations a rate with which a intermediate X undergoes rxn 2 may be sufficiently slow that the first rxn may b regarded as being at equilibrium.the exact condition for this is [W][X][Y].since this case corresponds to Arrhenius concept of an intermediate in eq with the reactants, such intermediate have being called Arrhenius intermediates. The converse case is that the condition is [X][Y]the concentration of X is small and the steady state treatment may be appliedto it. Intermediate of this kind have been called Vant Hoff intermediates. If neither of this of this extreme condition applies , the kinetic situation is more complicated , and the appropriate differential eq have to be solved. Only the equolibium and steady-state treatments are considered here. Equilibrium Treatment : Arrhenius intermediates In this case the equation : Applies. However , the concentration of C and S do not correspond necessary to yhe initial concentration [C] and [S]. Since appreciable amount of C and S have been used to form a intermediate X. These initial concentration may be expressed as [C]=[C] + [S] [S]= [S] + [X] As long as attention is confined to initial rates. Eq a become This is quadratic in [X] and can be solve for [X]. Yhen the expression for rate equal to k[X][W] , can be written down. However it os, more useful to consider two special cases. Case 1: if the initial conc of the substrate is much greayer than that of yhe catalyst, that is, if [S][C], it follows that [S] [X] is very close to [S], since [X] cannot exceed [C]. Eq b there fore reduces to : And thus The rate of rxn therefore V=[X][W]= This rate eq correspond toa variation of rate of all type represent .At lower substrate conc , when K[S][Y], the rate become independent of [S], as long as the condition [S]>>[C] holds, however the rate varies linear with [C]. This type of behaviour is characteristic or single-substrate rxn on surfaces and of enzyme rxn. For both of these the species Y and W are nonexistence and eq c become: The eq is also eq to the Michaelis Menten eq for enzyme rxn. This eq usually written Where is the Michaelis const , is equal to 1/k in the present treatment. In rrn catalysed by acid and base it will be seen that the rate remain linear with the substrate concentration ; this is because of the special type of equilibrium that are rapidly established in the sol. Case 2: on the other hand , if the catalyst is greatly in excess of the substrate, that is [C]>>[S] eq a reduces to And the rate of rxn is The rate now varies linearily with the concentration of substrate , but the variation with the catalyst concentration . (b)The rate of reaction as a function of substrate conc for the case in which [S]>>[C] (a) rate of rxn as a function of catalyst concentration for the case[C]>>[S] Steady-state Treatment:Van,t hoff intermediate If the condition [W]>> applies, the concentration of X is small and the steady state treatment is available. The steady-state is substitution of [C] -[X] for [C] and of [S]-[X] for [S} gives since [X] is very small the term in can be neglected ; with its approximation above eq gives the rate is therefore this eq again indicates that at low conc of either catalyst or substrate the rate is proportional to either [C] or [S] ; at a higher concentration of either the rate become independent of that concentration . in catalyst by surface and enzymes , W and Y are nonexistence and the rate eq become An eq of essentially this form was first derived by Briggs and Haldane for enzyme reaction Catalyst By Enzyme Catalysis by enzyme , the biological catalyst , is much more specific than that by acids and bases. soe enzyme shows absolute specificity ; an eg is urease, which only the catalyzed of Urea. A lower degree of specificity is shown by such enzyme as the proteolytic enzymes, which catalyst the hydrolysis of the peptide linkage provided that certain structural condition are specified in the neighbourhood of the linkage.; this is known as group specificity. many enzyme exhibit stereochemical specificity, in that the catalyze the rxn of one stereochemical form and not the other.the proteolytic enzyme.The enzymes are protein but may be associated with non protein substance that essential to the action of enzyme.the action of enzyme shows some resemblance to the catalytic action of acids and bases but is more complicated. the present treatment of enzyme kinetics is confined to the influence concentration, ph, and temperature and to some brief comments about enzymes mechanisms. Measurement of the kinetics of biological systems at elevated temperatures utilizing flow techniques Continuous flow-type reactors have been used to study the kinetics of biological systems for quite some time. For continuous media sterilization, tubular flow reactors are particularly useful being simple in character and easy to control. However, one aspect quite often neglected in sterilization calculations is the residence time distribution of the reactor system. Serious errors in estimating the degree of bacterial destruction can be encountered if the residence time distribution is neglected; especially when a high degree of destruction is desired. This paper reports a study made to characterize and use the residence time distribution of a tubular reactor in the interpretation of high-temperature, short exposure time data for inactivation of Bacillus stearothermophilus spores. Mathematical models accounting for the residence time distribution of the tubular reactor have been proposed and employed to obtain high-temperature death-rate data.[14] Result Since enzymatic reactions are so important to biological chemical reactions, it is of great interest to be able to model them. By use of the study of chemical kinetics, it is possible derive rate equations for the steps involved in an enzymatic reaction. These rate equations are differential equations and can be used to model theconcentrations of each compound in the system. However, this system of differential equations is hard to determine experimentally because of the difficulty of determining the rate equations into theMichaelis-Menten enzyme equation. Many benefits stem from this transition. One benefit is the fact that it is now easy to determine the constants related to the enzyme equations. However, how do we know the Quasi-Steady-State Assumption is valid? It seems reasonable from a physical argument. Byuse of dimensional analysis, we can give a more rigorous mathematical argument for the Quasi-Steady-State Assumption. The Michaelis-Menten enzyme equation is very important i n the study of cellular systems by allowing a model that can be easily derived through experimentation. Summary Enzymes are single or multiple -chain proteins that act as a biological catalysts with the ability to promote specific chemical rxn under the mild condition that prevail in most living organism. All reaction in the body are mediated by enzymes, which are protein catalysis that increase the rate of reaction without being changed in overall process .than properties of catalyst in which Enzyme molecules contain a special pocket called a active site. Than the characterstic of enzymes where enzyme are organic compound produce by living organism. Thus we may define enzyme as organic catalyst produced by a organic cell. Then we studied the Enzyme Kinetics where studied the five equation:1 Michaelis-Menten Kinetics 2.Lineweaver-Burk Kinetics 3. Hanes-Woolf Kinetics 4. Eadie-hofstee 5. Reversible Inhibition.Than we studied the enzyme mechanism where studied two equations theSteady-state Treatment:Van,t hoff intermediate and the Equilibrium Treatment : Arrhenius intermediates.

Rental Income Essay -- Business, Taxes

In order to qualify as a REIT for any taxable year, at least 95% of a REIT’s gross income must be derived from sources such as dividends, interest, and 75% of income from items related to certain real property. The items of income related to real estate assets are listed under IRC  §856(c)(3) which includes, among other sources, rents from real property, interest on obligations secured by real property or on interests in real property, gain from the sale or other disposition of real property that is not inventory or dealer property, and dividends and gains from the sale or orther disposition of shares in other qualifying REITs. For the purpose of the income tests described above, IRC  § 856(d)(1) provides that the term rents from real property includes â€Å"rents from interests in real property, charges for services customarily furnished or rendered in connection with the rental of real property, whether or not such charges are separately stated, and rent attributable to personal property which is leased under, or in connection with, a lease of real property, but only if the rent attributable to such personal property for the taxable year does not exceed 15 percent of the total rent for the taxable year attributable to both the real and personal property leased under, or in connection with, such lease†. To provide guidance with regard to tiered partnerships, the Treasury prescribed Reg.  § 1.856-3(g) which states that a REIT is permitted to look through a partnership in which it is a partner for the purposes of applying the income tests of IRC  § 856(c)(2) and IRC  § 856(c)(3). This regulation section provides that a REIT is deemed to own a proportionate share of each of the assets of the partnership and that it is deemed to be ent... ...hall be issued to provide that certain items of gross income will not be taken into account in determining income or loss from any activity. The court could not justify treating IRC  §469(l)(1) as self-executing and IRC  §469(l)(2) as not being self-executing. The court stated that there was intent to promulgate regulations to carry out a statutory purpose and the fact that regulations are not forthcoming cannot be an acceptable basis to preclude taxpayer from congressionally intended and appropriate relief. In addition, the court emphasized that Hillman’s approach in netting his share of self-charged management fee expense with gross income from the activities fulfills the economic significance concern. The taxpayer did not experience accretion in wealth. The court did not see an economic difference between this situation and one involving self-charged lending.

Insider trading about Martha Stewart

When she was young, Martha committed her attempts to school assignments, obtaining report books full of best marks. She gained a scholarship to Barnard College, where she employed as a model and wedded with a law scholar, and changing her name becomes Martha Stewart. She discontinue her career as model when she was pregnant. Then she worked as a broker for few years. She was pretty good in doing the job, so she would have recognized about insider trading laws (â€Å"Martha Stewart, broker indicted†, 2003).When she was a college student, Stewart involved in business with her friend. Stewart began a catering business. Her catering business became productive and successful. Stewart started a retail store and sold her home equipments. She co-wrote a best-seller book, entertaining peoples, with long-period fashion ace Elizabeth Hawes. She began cropping up on Television talk shows with confidential information for troubled housewives. She was also having crucial problem with her hu sband. After Stewarts divorced, her husband married the worker. In the meantime, Martha Stewart's business remained successful (â€Å"Martha Stewart, broker indicted†, 2003).Stewart launched her magazine, Martha Stewart Living, in 1991. It became an achievement. Two years later, she began her own TV show, Martha Stewart Living. Initially, the insiders were unsure it would run well, but surely it was become tremendously rewarding TV show. Stewart generated a lot of money increasingly at that period (â€Å"Martha Stewart, broker indicted†, 2003).Insider Trading in case of Martha StewartThe Securities and Exchange Commission, in 2002, informed that Martha Stewart was investigated for insider trading case. In December 2001, she had sold 3,928 shares of ImClone Systems merely ahead the Food ; Drug Administration informed that it was entrancing ImClone's utilization to sell a modern supposed wonder medicine. It seemed like standard insider trading, and it believably was (â⠂¬Å"Stephen Moore on Martha Stewart & Insider Trading†, 2004).However, inquisitively the federal officials never testified this in courtyard, or even attempted to establish it. Alternatively, they appointed Stewart with four law-breaking, such as confederacy, construction of natural virtue, and two numbers of creating incorrect statements to officials. A jury said that she is blameworthy, and she was decided to be prisoned for five months. They thought that it is a law-breaking to telling the falsity to a fed. The speech communication does not have to be recorded, and witnesses are elective (â€Å"Stephen Moore on Martha Stewart & Insider Trading†, 2004).Martha Stewart has been in the news program and media for some months because the U.S. Securities and Exchange Commission considers that she was confirmed by Sam Waksal that his company ImClone’s cancer medicine had been declined by the Food and Drug Administration earlier than this report was published (Schroede r, J., 2004).This state of affairs was a great stroke to his company and the monetary value of its stock descended spectacularly. Nevertheless, Martha Stewart was not monetary injured because she had her stock broker sell her 4000 shares earlier than this information was published. If it is accurate, and it should be lined it has not been evidenced yet, and so she is chargeable of insider trading. The Stewart beliefs should make a resentful after-sensation in conservatives' openings for other causes. Stewart was a unfortunate person of socio-economic class conflict that has filtered down from the unintelligent (Schroeder, J., 2004).One of the panelists remarked joyously that this final judgment was warrantied, because it would bring a subject matter to the â€Å"valuable and strong†, which they cannot escape with such maltreatments. The print media also pleasured in performing the â€Å"socio-economic class conflict   correspondence† by spiting Martha Stewart for suc h wrongdoings as dressing high-priced jewelry at the time of the legal proceeding (â€Å"Stephen Moore on Martha Stewart ; Insider Trading†, 2004).Stewart now confronts possibly two years in correctional institution and the termination of as a minimum one-half of her financial condition, all because she handled to preserve herself $50,000 selling ImClone stock at the time of she perceived that one of the medicines the companies had been expanding had unsuccessful to acquire FDA acceptance (â€Å"Martha Stewart Stock Scandal†, 2003).In conclusion, Martha Stewart has been one of the great and victorious entrepreneurs of this contemporaries era. She produced hundreds of millions of dollars of innovative economic condition and nearly an innovative business enterprise that was effectively by herself. She made many occupations and was a booming enterpriser who materialized to produce much money.The origin my edginess is that a number peoples in our social group praise her ru ination incisively because of her tremendous attainment. However, attainment is a moral excellence in United States, and while the people begin handling it as frailty, they minimize their competitive arrangement. And so they have an untold greater difficulty in their social group than whether people are exchanging on active stock confidential information among the period of time.BibliographyMartha Stewart, broker indicted. 2003. [Online]Available at: http://money.cnn.com/2003/06/04/news/martha_indict?cnn=yesMartha Stewart settles SEC's insider trading case. 2004. [Online]Available at: http://redorbit.com/news/general/605372/†¦/index.htmlSchroeder, J. 2004. SSRN-Envy, Jealousy and Insider Trading: The Case of Martha Stewart. [Online]Available at: http://papers.ssrn.com/sol3/papers.cfm?abstract_id=419580SEC Charges Martha Stewart, Broker Peter Bacanovic with Illegal Inside. 2003. [Online]Available at: http://www.sec.gov/news/press/2003-69.htmStephen Moore on Martha Stewart & Insi der Trading. 2004. [Online]Available at: http://www.nationalreview.com/moore/moore200403090901.asp

The Minimum Wage is Bad - Free Essay Example

Sample details Pages: 5 Words: 1582 Downloads: 8 Date added: 2019/04/16 Category Law Essay Level High school Tags: Minimum Wage Essay Did you like this example? The Minimum Wage is Bad The state of Arkansas this past November on the voting ballot was the choice for citizens to vote for the raising of the minimum wage to $11.00/hr over the next three years. At first glance, someone might think that this is a rewarding change but when taking a deeper look into the subject, it will reveal a lot of consequences that will cause a lot of trouble over time. Cost of living is going to rise, businesses will be less likely to hire when needed, unemployment numbers will rise and simple things such as a hamburger at McDonalds will go up.. Don’t waste time! Our writers will create an original "The Minimum Wage is Bad" essay for you Create order Currently the minimum wage in the southern United States averages around $8.00/hr.(LaborLawCenter) This is the reason housing is so much cheaper in the south than living in California where the minimum wage is $12.00 or New York where it is $11.00. Now imagine this, Arkansas having the same minimum wage as New York. There are four major entities that affect cost of living; housing, taxes, healthcare, food. The average rent for a 1,000 sq.ft. apartment is roughly $3500 where the same size apartment will run you around $800 in Arkansas (RentCafe.com). Housing cost 379% more in New York when compared to Arkansas. Health insurance rates will skyrocket as well. The average health insurance for Arkansas is right around $2800 (Valuepenguin.com) with New York coming in over double the price with at $6800.(Empirecenter.org) When businesses raise a minimum wage, theyre also having to give raises to the employees who make more than minimum wage. Who wants to go to a four-year school, spend thousands of dollars for classes and then come out making $15/hr for a nursing job when they could go flip burgers at the local burger joint for $11 and not be liable for someones life? When employees get raises, then the cost of goods rise as well affecting the overall cost of living. Along with cost of living going up, there will be a rise in the unemployment rate as well. It is simple economics when it comes to this aspect of raising the minimum wage. Non-skilled labor jobs are easy to come by. An employer will pay X amount to this position. When the wage gets over that threshold, the employer will be less likely to hire for this position. What this equals is that position going away altogether, instead of being paid a lower wage. Now that job along with the services it provided are gone. Economist Richard Vedder quotes If the price of something rises, people buy less of it including labor. Thus governmental interferences such as minimum-wage laws lower the quantity of labor demanded. What he is saying is basically clarifying what is written above. On February 2017, Wendys CEO Bob Wright states there is a 4% increase in wages across the board in his company. First, they could cut margins, but with an 8% margin, thats unlikely. The second option is to raise prices. Given how price-sensitive consumers are these days, that too is a non-starter. Finally, the firm could reduce the amount of labor they use and thats exactly what they did. Wendys eliminated 31 hours of labor per location, per week.(businessinsider.com) Now, the whole purpose of raising the minimum wage was really aimed at this market of employees which are the non-skilled jobs. Well, now that they have cut hours but the business is open so what now. Wendys CIO David Trimm states they will be installing automated ordering kiosk into 16% of their stores by the end of 2017 and their machines would pay off in a two year time frame because of the savings by reducing wages. Wendys is not the only one going to the automated route. McDonalds is going the automated route also specifically in the New York and Seattle Markets.(businessinsider.com) Why those markets? Because they have some of the highest minimum wages in the nation. As long as states continue to raise minimum wage, these low skilled jobs will be killed off. In a survey of 1,213 businesses and human resources professionals, 38% of employers who currently pay minimum wage said they would lay off some employees if the minimum wage was raised to $10.10.(https://minimum-wage.procon.org) Thats not even $11.00 an hour or an even higher wage as some think it should be. Taking an educated guess, that number would be pushing 50% at $11.00. If there is a company ten employees making minimum wage at $10.10, that is $404 a week. Going up to $11 would mean an additional $36 a week. Given that employee is full time and works a full forty hour work week. They would make an additional $1,872 a year for one employee. Now the company has ten employees, that is a humongous increase of nearly $19,000. Depending on the business, that could be the entire budget for the year. Now that company is having to layoff to afford to pay rent, utilities, and insurance on their building. For a small business paying ten high school kids $8.50/hr for 17 hours a week. That is $1,445 per week and $75,140 for the year. With the increase to $11/hr that yearly figure now goes up a whopping $22,100 for the year. The employer is going to cut hours and/or employees to get that cost back down to a manageable figure. Minimum wage jobs are aimed at students and young adults that are making money while furthering their education. 50.4% of all minimum wage jobs are held by kids and young adults aging from 16 24. Most employers are going to be less likely to hire a 16 year old high school student for $11/hr that they deem worthy of $8.50/hr. There is a catch phrase used commonly when talking about minimum wage and that is you cant raise a family on minimum wage Minimum wage is not designed to raise a family on. It was created in 1938 by President Roosevelt and was intended to deliver fair labor standards throughout the country(historynewsnetwork.org) The unemployment rate for ages 16-19 is roughly 20%, increasing the minimum wage is only going to make this number go up. A lot lower than other age groups proving that a high minimum wage is causing employers to not hire unskilled workers. In 2009 whe n Chicago raised their minimum wage, there was a 9% spike in teenage unemployment in three months. According to a study by Thomas A. Mroz, PhD, and Timothy H. Savage, PhD, for the Employment Policies Institute, those experiencing unemployment at an early age have years of lower earnings and an increased likelihood of unemployment ahead of them. Teenagers and young adults need jobs at their age to teach them life values like going to work when you really do not want to, getting along with co-workers when times are rough and the feeling of accomplishment of finishing a project or goal at a job. Without these, there would be a lot more unemployed teenagers which is only going to lead to higher crime rates and more unemployed adults. The last example of why a higher minimum wage is bad is the cost of goods will increase. Other than automation which was discussed earlier the establishment is going to pass the rising labor cost onto the consumer at a 100%. Higher wages in hotels are going to cause an increase in guest rooms and meeting rooms. A simple cup of coffee in Oakland, CA rose 10-20% when the rate was increased to $12.25. When the minimum wage was raised to $10 in Chicago, a cup of coffee jumped 6.7% (NBCNews.com). Hamburgers are either going to increase in price or the size of the patty is going to decrease to help offset the labor cost. In closing, there have been several examples discussed of why raising the minimum wage is not a great idea. It is not designed to live on nor provide for the family. It will only make the the low income individuals fall into poverty level income. It will push employers to either lay off workers or close up business completely. Teenagers are less likely to find work which will lead to higher dropout rates of school, higher crime rates and even more of a percentage of citizens unemployed and living in poverty followed by the skyrocketing of the cost of living in general. The minimum wage should be used as a floor of wages and utilized as a stepping stone in the workforce and not a way of living forever. Work Cited 2019 Minimum Wage Rates by State. Labor Law Education Center: Learn About Labor Laws in Your State, www.laborlawcenter.com/state-minimum-wage-rates/. Little Rock, AR Rental Market Trends. Apartments for Rent RENTCaf, www.rentcafe.com/average-rent-market-trends/us/ar/little-rock/. Cost of Living Comparison: Compare Spokane, Washington to Rancho San Diego, California, www.bestplaces.net/cost-of-living/little-rock-ar/new-york-ny/81000. NY Health Insurance Costs Surge. Empire Center for Public Policy, www.empirecenter.org/publications/new-yorks-health-insurance-costs-surge/. Kwak, James. The Curse of Econ 101. The Atlantic, Atlantic Media Company, 14 Jan. 2017, www.theatlantic.com/business/archive/2017/01/economism-and-the-minimum-wage/513155/. Research, Garret/Galland. Minimum Wage Hikes Are Causing Businesses to Cut Jobs. Business Insider, Business Insider, 16 Mar. 2017, www.businessinsider.com/minimum-wage-leads-to-job-losses-2017-3. Goddard, Alexander. Why Was the Minimum Wage First Established? History News Network, historynewsnetwork.org/article/164635. Flows, Capital. Lets Eliminate The Minimum Wage For Teenagers. Forbes, Forbes Magazine, 7 Apr. 2014, www.forbes.com/sites/realspin/2014/04/07/lets-eliminate-the-minimum-wage-for-teenagers/#1a7ce3377255. The Long-Term Effects of Youth Unemployment. Employment Policies Institute, www.epionline.org/studies/r51/. Cost of Cup of Coffee Often Climbs After Minimum Wage Hikes. NBCNews.com, NBCUniversal News Group, www.nbcnews.com/business/consumer/cost-cup-coffee-climbs-after-minimum-wage-hikes-n394076.