Assignment Biochemistry
Assignment Biochemistry
Introduction:
Enzymes are proteins that act as a catalyst in living organisms, and it is responsible for many
essential biochemical reactions that keep a person alive and well, such as digestive food and
much more. Additionally, our bodies independently manufacture the enzymes.
Functions:
Enzymes assist in specific processes that are essential for body function and overall health. One
of the functions of enzymes is that they play a role in the digestive system. Digestive enzymes
come in a variety of forms, including amylase, maltase, lactase, lipase, proteases, and sucrase.
For example, the enzyme amylase is essential for the breakdown of carbohydrates, the enzyme
maltase converts maltose to glucose, the enzyme lactase transforms lactose into the simple sugars
galactose and glucose after breaking down lactose, the enzyme lipase is in charge of the
breakdown of fats into fatty acids and glycerol, the enzyme sucrase helps the process of
switching sucrose into glucose, and the enzyme protease breaks down proteins into amino acids.
These enzymes are substances that help us digest our food by breaking down large molecules
into small molecules, to allow the body to use them as fuel.
Kinetics:
Enzyme kinetics is to determine the rate of a reaction and how it changes in response to changes
in experimental parameters. The purpose of enzyme kinetic is to study the enzyme behavior, and
how variables like substrate concentration, enzyme concentration, temperature, pH, and the
presence of inhibitors or activators impact the rate of an enzyme-catalyzed reaction. When the
substrate concentration is low, the reaction rate increases linearly and is directly proportional to
the substrate concentration. However, at higher substrate concentrations, the reaction rate reaches
a maximum and becomes independent of further increases in substrate concentration, as the
enzyme active sites become saturated. Competitive inhibitors compete with the substrate for
binding to the enzyme's active site, while non-competitive inhibitors bind to a different site on
the enzyme, causing a conformational change that reduces its activity.
Mechanism:
Enzymes can catalyze biochemical processes in a variety of ways. Here are descriptions of some
common mechanisms utilized by different types of enzymes:
4. Lyases: Lyases catalyze reactions where chemical bonds are broken or formed to produce
a double bond or a ring structure without the involvement of water or redox reactions.
They can catalyze addition, elimination, or group transfer reactions. Lyases are involved
in processes such as the conversion of pyruvate to acetaldehyde in the glycolytic
pathway.
6. Ligases: The combining of two molecules is catalyzed by ligases, which frequently also
catalyze the hydrolysis of ATP. They are involved in processes such as DNA replication
and the synthesis of macromolecules. Ligases are also known as synthetases or synthases.
Each enzyme operates through specific mechanisms that are tailored to their specific substrates
and reactions. Enzymes can also employ coenzymes, cofactors, and prosthetic groups to assist in
catalysis and provide additional functionality. The precise mechanisms employed by enzymes
are a subject of ongoing research and are crucial for understanding the intricate workings of
biochemical reactions in living organisms.
References:
https://www.britannica.com/science/enzyme
https://teachmephysiology.com/biochemistry/molecules-and-signalling/enzyme-kinetics/
https://www.ncbi.nlm.nih.gov/books/NBK9921/