ENZYMES ENZYMES SUBSTRATE COMPLEX MODEL INDUCED FIT MODEL
7.9.2. Induced fit model : It was proposed by Koshland, according to this model active site of enzyme are flexible they can be change according to the shape of the substrate that is active site does not possess a rigid structure.
7.10. Factors that Affect the Rate of Enzyme Reactions
Enzymes function optimally at a particular temperatures. As temperature increases, kinetic energy increases and collision increase and more molecules now have sufficient energy to overcome the activation energy. The enzyme reaction rate increases with an increase in temperature but as the temperature rises above optimum temperature, the denaturation of enzyme starts. Once it is denatured, the enzyme’s three dimensional structure is lost. The enzyme’s shape changes, therefore the three dimensional shape of its active site changes as it cannot bind to the substrate anymore and the enzyme cannot function furthermore. Therefore, at higher temperatures the enzyme’s reaction rate decreases.
The optimal temperature for an enzyme is the temperature at which the enzyme “works best” and the rate of chemical reaction is highest. The “optimal temperature” for most of the enzymes in the body is 98.6 degrees F (also known as ~37 degrees C).
The increase in rate with temperature can be quantified as the Q10, which is the relative increase for a 10°C rise in temperature. Q10 is usually around two for enzyme-catalysed reactions (i.e. the rate doubles every 10°C) and usually less than two for non-enzyme reactions.
7.10.2. Effect of pH
Enzymes function optimally at a certain pH. They are extremely sensitive to changes in acidity and works within quite narrow pH range. Changes in pH can make new bonds with substrate and break the existing bond within the enzyme. This leads to change the shape of the enzyme. If the pH is too low (too acidic) or too high (too basic), the enzyme becomes denatured. Enzymes is made up of amino acid. The charge on protein depends upon pH. Change in pH change the charge on enzyme which affects its binding with substrate and also changes the existing three dimensional structure of enzyme. The chemical bonds within the enzyme are rearranged. As the enzyme’s shape changes, the three dimensional shape of its active site changes and the active site cannot bind to the substrate anymore. Thus, the enzyme cannot function anymore. The “optimal pH” for most of the enzymes in the body is ~pH7.4. However there are exceptions, such as the digestive enzymes of human stomach function at pH of 3-4.
7.10.3. Effect of enzyme concentration
When substrate [S] is not limiting then under these conditions an increase in enzyme [E] has a direct effect on the rate of reaction. A plot of rate of reaction [v] versus [E] results a straight line.
7.10.4. Substrate concentration :
The rate of reaction is also depended upon substrate concentration. However it depends upon the total number of active site present on enzyme. At a particular enzyme concentration increase in the substrate concentration increase the rate of reaction in the begining but once all the active site of a given enzymes is saturated by substrate there is no further increase in the rate of reaction. The maximum rate of reaction is known as Vmax. i.e. the rate of reaction is saturated as there is no change in the rate of reaction on further increase in substrate concentration. The Vmax is directly proportional to the total enzyme concentration (E).
- Book COVER AND ABOUT US
- CHEMICAL BONDING
- AMINO ACIDS
- PROTEIN STRUCTURE
- RAMACHANDRAN PLOT
- PROTEIN STABILITY
- KINETIC ANALYSIS
- REGULATION OF GLYCOLYSIS
- TRICARBOXYLIC ACID CYCLE (TCA CYCLE)
- REGULATION OF THE CITRIC ACID CYCLE
- GLYOXYLATE CYCLE OR KREBS KORNBERG CYCLE
- ELECTRON-TRANSPORT CHAIN
- MECHANISMS OF OXIDATIVE PHOSPHORYLATION
- PENTOSE PHOSPHATE PATHWAY
- LIPID METABOLISM
- FATTY ACID OXIDATION
- DNA STRUCTURE
- NUCLEOTIDE BIOSYNTHESIS