Enzymes are referred to as biological catalysts because they are going to enhance the rate of reactions. So the enzymes are synthesized in our living cells, and these are low molecular weight proteins.
The majority of enzymes in our body are proteins, with certain exceptions. Like some of the RNA is also a somatic activity, and the example for that is Ribose. Today we are going to learn about the mechanism of enzyme action and how do enzymes work. Let’s start our lecture.
How do enzymes work?
Enzymes are protein molecules, and they are made up of amino acids. They are the catalysts of biological origin that accelerate the various biochemical reactions in biological systems.
Almost every biochemical reaction is catalyzed by an enzyme-like all other catalysts enzymes, increasing chemical reactions without being consumed or permanently altered. However, they differ from ordinary chemical catalysts in:
- Higher catalytic power (Higher reaction rates).
- Greater reaction specificity.
- Milder reaction conditions.
- Capacity for regulation.
Few non-biological catalysts have all these properties. However, their catalytic mechanism employed by enzymes is identical to those used by chemical catalysts.
Enzymes are better designers and are biologically relevant conditions, and catalyze reactions tend to be slow.
Mechanism of enzyme action: Lock & Key Hypothesis
What are the lock and key hypotheses? It is related to the relation between substrate and enzyme. The substrate can be referred to as a key. The enzyme’s active site can be referred to as lock and thus key and lock mechanisms.
It indicates that the substrate has a complementary shape of complementary shape with the enzymes’ active site. It means only a specific substrate can fit it. They are quite specific reactions because only a specific substrate can bind to the specific active site. Not any substrate can bind to any active site.
The lock and key model is the induced fit model that describes how our binding occurs more correctly. The substrate fits precisely and correctly into the active side to complement their complementary shapes in the lock and key model.
When they fit, this moves into the active side, forming those non-covalent interactions. According to our induced fit model, the enzyme’s active site is not complementary to our substrate. Still, when the binding takes place, the enzyme conforms to the structure of that substrate. So the enzyme’s active site changes shape ever so slightly.
In the induced fit model, the shape of the enzyme’s active site is not exactly complimentary. However, upon binding the substrate to the active site, the binding causes the active site to complement the substrates. The induced-fit model tells us it is when the binding occurs at the active site of that enzyme.
So the substrate becomes complementary to the active side, and the active site becomes complementary to that particular substrate. The induced-fit model correctly describes how the binding occurs between the enzyme and the substrate’s active site.
The catalytic activity of enzymes involves their binding or their substrates to form an enzyme-substrate complex. The substrate binds to a specific region of the enzyme called its active site. The substrate is converted into the product of the reaction, releasing it from the enzyme.
A peak denotes the transition state. The difference between the ground state’s energy levels and the transition state is called a Gibbs free activation energy. Or simply the activation energy it is denoted by Delta G.
Here are 5 methods to describe the mechanism of the enzyme.
Let us study non-covalent interactions between enzyme and substrate, like non-covalent bonds and hydrogen bonds, hydrophobic, ionic interactions. These interactions are accompanied by a release of free energy called binding energy.
This binding energy contributes to has a specificity as well as to catalysis. Much of the catalytic power of enzymes is ultimately derived from this binding energy. As it is a significant source of free energy used by enzymes to lower the activation energies of reactions as per equation,
V= k [S] = kT/h [S] e^-∆G/RT
About 5.7 kilojoules per mole must lower g to accelerate the first-order reaction by a factor of 10 under conditions commonly found in cells. The energy from forming a single weak interaction is generally estimated to be 4 to 30 kilojoules per mole.
Therefore, many such interactions’ overall binding energy level is sufficient to lower activation energies by 6,200 kilojoules per mole. The same binding energy that provides energy for catalysis also gives an enzyme.
We have all these different types of enzymes found inside our bodies. They decrease the reaction’s activation energy, but how exactly is that achieved, and what are some mechanisms. What are some methods that enzymes use to achieve this decrease in activation energy?
Many enzymes contain active sites with catalytic residues that can form temporary covalent bonds with the substrate molecule. They also keep that molecule in place for the time being until that reaction takes place.
The enzyme is never used or depleted, or changed in any reaction. We have to break that bond, and that’s exactly why we call this bond a temporary or a transient covalent bond. For example, some enzymes such as trypsin, chymotrypsin, and other digestive enzymes as well.
In this reaction, in the first step, this molecule forms a bond between the oxygen and this carbon kicking off this terminal amino acid to form the following temporary, transient acyl intermediate molecule. At the end of the reaction, this bond is broken.
It forms the bond to keep this group attached to the active site so that another substrate can move in and grab this group. So the bacterial enzyme glycol peptide transpeptidase utilizes covalent catalysis. Chymotrypsin is an important digestive enzyme that exists inside the digestive system.
Catalysis by proximity
By collision theory, two substrate molecules that are about to react must collide. They must collide with enough energy and with the proper orientation.
When the collision occurs with the proper orientation and the right amount of energy, do we form the product molecule? They bring the substrate molecules into the tiny space that creates a microenvironment for that reaction.
So inside the active site, they create a microenvironment that brings those substrate molecules nearby, but it also orients those subject molecules in the proper orientation.
- Many biological reactions involve two or more substrate molecules. This implies that for reaction to take place. They must be close enough and must also have the proper orientation.
- Active sites provide a microenvironment that brings the substrate close enough for the collisions to occur at a high enough frequency. The active sites may also orient the molecules in the proper orientation for that bond to form and form those products.
Many residues are involved, or specific residues are found in active sites that transfer an H ion. One specific residue is the histidine amino acid.
So the histidine molecule has a pH that is relatively close to the normal physiological pH. Active sites may contain residues such as histidine that can participate in transferring hydrogen ions.
If a hydrogen ion transfers from one molecule to another molecule, it creates a strong nucleophile. And that strong nucleophile might be needed in that particular biological reaction.
By transferring the hydrogen ion, the active site may activate a nucleophile required in that catalysis process. Also, It can stabilize different types of groups that might be found inside the activities that contain charges.
And the transfer of hydrogen ions can use to increase the electrostatic interactions within that active site. It can, in turn, stabilize things like the transition state inside that chemical reaction.
Example: Now, one particular example of an enzyme that uses acid-base catalysis is chymotrypsin. Inside the chymotrypsin active site, there is serine residue that acts as a nucleophile.
The hydrogen ion from the oxygen of serine must take away. The hydrogen atom is transferred onto the nitrogen. The positive charge is essentially delocalized among these different atoms in the histidine side chain. But this one now contains a full negative charge.
The mechanism by which enzymes can decrease the activation energy and increase reaction rates is called metal ion catalysis. Example: myoglobin and hemoglobin. These proteins use metal atoms, and in fact, enzymes utilize metal as cofactors.
What’s so special about these metal of metal atoms? Metal atoms can lose electrons very quickly, and by losing electrons, they gain a positive charge. So they are deficient in electrons.
They have a positive charge, which can interact with different types of molecules found inside the active site. They can stabilize the transition states and the intermediate molecules that are formed within that active site.
Example: Zinc metal atom is used to form a strong nucleophile. The hydroxide nucleophile and metal atom can be used to hold that substrate molecule in place.
So, in the same way, we can use covalent catalysis to orient that substrate and hold it in place. We can also use the positive charge of these metal atoms to bring the substrate molecules in the proper orientation and hold them inside the active site so that reaction can occur at a reasonably high rate.
Enzymes are the biological catalysts that speed up the rates of all different types of reactions inside our cells. I hope you will understand the working principle and mechanism of enzymes properly. If you have any questions, then please ask me in the comment section.
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