|
|
This is only a preview of the paper
Click here to register and get the full text.
Existing members click here to login
|
|
|
Introduction
Scientists have studied enzyme reactions in great detail over the years and have successfully determined the details of certain enzyme-catalyzed reactions. ... However, before these steps can be taken, a detailed understanding of the various factors influencing enzyme-catalyzed reactions must be researched, and this is easiest done on reactions that are widespread throughout nature. ... By oxidizing Dopa, Tyrosinase aids in reducing the number of electrons thereby releasing energy, which the cell can use for other functions. ... Enzymes are highly specific due to their three dimensional shape and therefore have the ability to interact with the reactants forming an enzyme-substrate complex and can push forward the reaction by manipulating the electrons, by physically bending, or by changing the proximity of the reactants within the complex’s active site environment; this lowers the energy of the molecules’ transition state which essentially lowers the reaction’s activation energy. After the products are formed the enzyme interacts with new reactant molecules (Alberts et al. ... Factors manipulating an enzyme’s activity rate, the time it takes to change a known amount of substrate into product, include temperature, pH (Campbell et al., 1999), along with substrate and enzyme concentrations (Alberts et al. ... Temperature manipulates an enzymes ability to interact with a substrate by increasing the rate at which the substrate finds its way to the enzyme’s active siteThe enzyme and the substrate molecules exhibit an increased velocity as temperature nears the enzymes’ optimal point as the substrate particles collide with the enzymes’ active sites at increased speeds. Above this critical point, the hydrogen, ionic, and other weak bonds stabilizing an enzymes three dimensional shape are broken and the enzyme is denatured and ceases to function. Similarly an enzyme also operates at an optimal pH, where a highly basic or highly acidic environment may disrupt an enzymes active confirmation by destroying the bonds holding together the enzymes’ three-dimensional shapes (Campbell et al. ...
The influence of substrate concentration on enzyme activity can be explained from Equation 1 where R is equal to the rate of reaction, S is the substrate concentration, Vmax is the maximum reaction rate, and Km is the substrate concentration where the enzyme works at half its maximum rate (Alberts et al. ... Note that this equation does not explain the impact of enzyme concentration on reaction rates. ... Note that a low Km indicates a tight enzyme binding with substrate whereas a high Km indicates a loose enzyme binding with substrate (Alberts et al. ...
Colorimetry is a widely used tool for examining enzyme reactions.
Approximate Word count = 2092
Approximate Pages = 8.4
(250 words per page double spaced)
|
|
|
|
|
|