Question

The variation of the rate of an enzyme catalyzed reaction with substrate concentration is correctly represented by graph

• A.
• B.
• C.
• D.

Hint:

The rate of enzyme reaction is directly proportional to the substrate concentration.

Answer 1

The Correct Option is C

The graph representing the variation of the rate of an enzyme-catalyzed reaction with substrate concentration follows Michaelis-Menten kinetics. Initially, the rate of reaction increases linearly with substrate concentration as active sites on the enzyme are free and readily available. However, as the enzyme becomes saturated with substrate, the rate reaches a maximum (V$_max$) and remains constant, regardless of further increases in substrate concentration. Graph (c) best represents this relationship as it shows:
- An initial linear phase where the reaction rate increases.
- A plateau phase where the reaction rate becomes constant due to enzyme saturation.
The reaction rate of an enzyme-catalyzed process depends on the concentration of substrate. At low substrate concentrations, the reaction rate is proportional to the substrate concentration. At high concentrations, the enzyme becomes saturated, and the reaction rate levels off at V$_max$, indicating that all enzyme active sites are occupied.

Answer 2

The correct answer is Option C) 

Real Life Applications

Processing of Food Industry 
Enzymes are primarily employed in the food sector to process the raw ingredients required to make a variety of goods, including dairy, bread, meat, beer, and wine products. In addition to this typical function, enzymes are also utilised in the manufacture of several food items and alcoholic drinks. Enzymes are employed in food manufacturing as well as to enhance the food's quality, including its colour, flavour, and taste. industry of pharmaceuticals Enzymes are now widely used as medications due to the influx of new technology and special properties of enzymes. These medications offer an unmatched potential and benefit over other common tiny molecular drugs since they selectively attach to targets. 
Enzymes are used to cure a variety of deadly and infectious disorders, including allergies, heart attacks, viral and bacterial infections, inflammation, skin ulcers, leukaemia, thrombosis, plague outbreaks, and many more as a result of this special property.
Industry of Textile Processing and Fabric Finishing. Nearly 400 to 500 common consumer and industrial items are produced and improved using enzymes. 
Enzymes may be utilised to create a variety of ecologically beneficial goods, helping to maintain a clean environment in the process. 
Enzymes also have practical uses in the laundry business to eliminate stains and lengthen the lifespan of clothes, in the paper industry to recycle paper and remove ink from paper goods, and in the FMCG industry to create dishwashing soaps and detergents. 
In addition to these typical uses, enzymes are also employed in the production of a wide range of foodstuffs, home goods, cleaning agents, biofuels, other types of automotive fuel, the processing of drinks, the textile sector, and even energy production facilities.

Question can also be asked as

• What is the shape of the Michaelis-Menten curve?
• How does the rate of an enzyme catalyzed reaction change with substrate concentration?
• What is the Vmax and Km of an enzyme?
• How can the Michaelis-Menten curve be used to understand enzyme kinetics?

Answer 3

The correct answer is Option C) 

The curve depicts how the concentration of the substrate affects the rate of an enzyme-catalyzed reaction. 

• It demonstrates that raising the substrate concentration raises the rate of reaction up until a point when all of the enzyme molecules' active sites are saturated with substrates, at which point raising the substrate concentration has no impact on the rate of reaction.
• The reaction rate would be slower if an enzyme inhibitor were present.
• The graph of the free energy level of the reaction mixture to the reaction's progression depicts the development of the enzyme complex.

Factors Affecting Enzyme Catalysis

• Above and below optimum pH and temperature ranges, the activity of the specific enzyme decreases.
• At first, as the substrate concentration rises, the reaction's speed increases, and then it reaches a maximum speed beyond which it can no longer go any faster.
• In order to accept certain modulator or effector molecules that eventually induce conformational changes in these allosteric enzymes and may possibly influence their catalytic activity, some enzymes contain an additional binding site known as an allosteric site or regulatory site.
• Certain inhibitor compounds have been shown to have a significant impact on the activity of a few different enzymes. These molecules attach to the enzymes either covalently (irreversible) or non-covalently (reversible), both of which reduce the catalytic activity of the enzyme.

Enzyme Kinetics

Enzyme kinetics, which primarily applies the Michaelis-Menten equation and is illustrated by the following equation and graph, determines the rate of an enzyme-catalyzed reaction and the creation of its products.

v = (V_max [S])/(K_m + [S])

V_max = The enzyme can only react at its highest rate under the present circumstances when the substrate concentration is infinite.. [S] = substrate concentration.

Also Read: 

Related Topics
Enzyme Properties	Enzyme Cofactors	Allosteric Enzymes