Examining The Four Inhibition Types In Enzymes Biology Essay

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As the term suggests, enzyme inhibitors are molecules that interact in order to prevent or slow down enzyme activity from taking place. Enzyme inhibitors can be broken down into various types depending on the location of the inhibitor attached to the active site which is where the enzyme reaction occurs, and the chemical process of inhibition. In general, inhibitors can be categorized into two groups: non-specific and specific inhibition. The first being, the inhibition in which the inhibitor will ultimately trigger denaturation of the protein portion which causes the reaction to be irreversible once it happens, and the latter being a case where a specific inhibitor will only function with a specific enzyme. Specific enzyme inhibition can again be divided into reversible inhibition and irreversible inhibition. An overlap forms between specific and non-specific inhibition regarding irreversible reactions, and depending on the characteristics of the enzyme, it can be categorized as either of the groups. Preventing an enzyme activity from erupting can exterminate a pathogen or correct the disequilibrium of metabolism. Given such characteristics, enzyme inhibitors are mostly used as drugs or also for agricultural purposes such as herbicides and pesticides, being used in various types of areas, and easy to discover, it is currently a popular subject of study in the field of biochemistry.

When a reversible inhibitor binds to the active site, the bond between the inhibitor and the enzyme is a multiple of weak bonds, therefore fragile, and easily removed by dialysis or dilution. Depending on how efficient the substrate, another protein portion that binds with the enzyme for catalysis to take place, is against the inhibitor, reversible inhibition can be grouped into four types: competitive, uncompetitive, mixed, and noncompetitive inhibition. Competitive inhibition is where the substrate and the inhibitor compete in order to access to the active site of the enzyme. This type of inhibition can be conquered by increasing the amount of substrate, thus out-competing the inhibitors. Uncompetitive inhibitors, easy to confuse with noncompetitive inhibitors, only bind to the substrate-enzyme complex and decrease the maximum velocity of catalysis, whilst non-competitive inhibitors reduces the enzyme activity, but does not affect the substrate binding the active site. Mixed inhibition takes place when both the inhibitor and the substrate are able to bind to the enzyme causing an allosteric effect, in which the inhibitor changes the shape of the active site causing the substrate to be attached to the allosteric site rather than the original, which will cause a completely different reaction. Substrate and product inhibition is a special case in which either the substrate or the product of enzyme reaction inhibits the enzyme��s activity.

Nonspecific inhibition functions the same way for any type of enzyme. For nonspecific inhibition the reaction rate increases proportionally with the temperature until it reaches the optimal rate, the maximum rate it can reach. At high temperature the protein part of the enzyme will begin to denature, thus inhibiting the reaction. The same applies to pH, the rate of reaction as the pH increases until it reaches a point where it will no longer increase.

The first step in inventing a new drug starts from the discovery of a new enzyme inhibitor. Previously, the only method of doing this was to go through trial-and-error. However, nowadays, with the progress of technology, using a rational dug design, it has become possible to predict if the shape of substrate and the inhibitor would actually fit the enzyme by observing the shape of the active site. With such things becoming possible, it is no surprise that the use of enzyme inhibitors in the field of pharmacology and biochemistry has increased. With the gain of popularity as a topic of research, other than the use from drug discovery, inhibitors have come in use for various purposes such as chemotherapy in genetics, metabolic control, pesticides and herbicides, and also as natural poison.

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As the term suggests, enzyme inhibitors are molecules that interact in order to prevent or slow down enzyme activity from taking place.

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Enzyme inhibitors can be broken down into various types depending on the location of the inhibitor attached to the active site which is where the enzyme reaction occurs, and the chemical process of inhibition.

ȿ�Ҿ�ff�� ��ff�� °ï¿½ï¿½ï¿½ï¿½'�� ����뿡 �پ� �ִ���, ��f��d������ ȭ���� ���?� ��� ���� ���� ~��� ������.

In general, inhibitors can be categorized into two groups: specific and non-specific inhibition.

�Ϲ���8��, ��ff�� ũ�� �� �׷�8�� ���� �� �ִ�: Ưd ��ff�� ��Ưd ��ff

The first being inhibition in which the inhibitor will ultimately trigger denaturation of the protein portion which causes the reaction to be irreversible once it happens.

ù��°ï¿½ï¿½ ���, ��ff�� �ᱹ �ܹ��� ����� ����; �ҷ��0� �°ï¿½, �ѹ� ����; ��8°ï¿½ï¿½ ����ų �� ��� �Ǿ���.

The latter being a case where a specific inhibitor will only function with a specific enzyme.

�ι�° ��: ���� Ưd�� ��ff�� Ưd�� ȿ�ҿ��� �����ϴ� ����̴�.

Specific enzyme inhibition can again be divided into reversible inhibition and irreversible inhibition.

�� Ưd ��ff�� �ٽ� ����·ï¿½ �ǵ��� �� �ִ� ��ff�� �׷��� ���� ���ϴ� ��ff �°ï¿½ï¿½ï¿½ï¿½ ������.

An overlap forms between specific and non-specific inhibition regarding irreversible reactions, and depending on the characteristics of the enzyme, it can be categorized as either of the groups.

����ų�� ��� ��ff�� ȿ���� ���� ��� Ưd ��ff Ȥ: ��Ưd ��ff�� �Ѵ� ���� �� �ִ�.

Preventing an enzyme activity from erupting can exterminate a pathogen or correct the disequilibrium of metabolism.

ȿ�ҹ���; �����ϴ� ��: �����; f���°Å³ï¿½, �������� �Ҿ�d��; ��d���ִ� ��� �ʷ��� �� �ִ�.

Given such characteristics, enzyme inhibitors are mostly used as drugs or also for agricultural purposes such as herbicides and pesticides, being used in various types of areas, and easy to discover, it is currently a popular subject of study in the field of biochemistry.

�̷��� ����� ������, ȿ�� ��ff�� ���̳� f��f�� ����f ��: ����� ����8�� ���̱⵵ �Ѵ�. �پ��� �о߿��� �?��� �����°ï¿½, �°ï¿½ï¿½Ï±ï¿½ ���ٴ� a ������ ȿ�� ��ff�� ��� ��ȭ�п��� �α⸦ ��� �ִ� ��f�̴�.

When a reversible inhibitor binds to the active site, the bond between the inhibitor and the enzyme is a multiple of weak bonds, therefore fragile, and easily removed by dialysis or dilution.

����; ����ų�� �ִ� ��ff�� °ï¿½ï¿½ï¿½ï¿½'�� ������ �� ���� ���� ���� ������ ���µï¿½, �̴� ���̳� ��8�� ���� f���� �� ��; d���� ���ϴ�..

Depending on how efficient the substrate, another protein portion that binds with the enzyme for catalysis to take place, is against the inhibitor, reversible inhibition can be grouped into four types: competitive, uncompetitive, mixed, and noncompetitive inhibition.

ȿ�ҿ��� �˸����; '�� �ʿ��� ������ ��ff�� �����ؼ� �󸶳� È¿2������ ��� �°ï¿½ï¿½ï¿½ ~��� ������: competitive, uncompetitive, mixed, and noncompetitive inhibition�̴�.

Competitive inhibition is where the substrate and the inhibitor compete in order to access to the active site of the enzyme.

Competitive inhibition������ ����� ��ff�� °ï¿½ï¿½ï¿½ï¿½'�� �����ϱ� '�� ����; �Ѵ�.

This type of inhibition can be conquered by increasing the amount of substrate, thus out-competing the inhibitors.

�̷��� ��f�� ������ ��; ����Ѽ� ��ff�� °ï¿½ï¿½È­ï¿½ï¿½ �� ��� �� �� �ִ�.

Uncompetitive inhibitors, easy to confuse with noncompetitive inhibitors, only bind to the substrate-enzyme complex and decrease the maximum velocity of catalysis, whilst non-competitive inhibitors reduces the enzyme activity, but does not affect the substrate binding the active site.

Uncompetitive inhibitors�� noncompetitive inhibitors�� �°ï¿½ï¿½ï¿½ ����, ���ڴ� �˸������ �ִ�ӵ��� ����ٴ� a����, ���ڴ� ȿ�ҹ���; ���ҽ�°ï¿½ï¿½ï¿½ ����, ������ ȿ�Һ�'�� ������ �� ���� ����; ��ġ�� �ʴ´Ù´ï¿½ a���� ��: Ȯ���� �ٸ���.

It alters the shape of the active site so that the substrate can��t react with it, causing the substrate to react with another active site created by the inhibitor, which is generally located close to the original site.

ȿ�Һ�'�� ���; ������Ѽ� ������ ����; ��8°ï¿½ï¿½ ���ϵ��� �ϴ� ���̴�. ��ff�� ���� ��� ��ܳ� ȿ�Һ�'��, �ַ� �� �ִ� ȿ�Һ�' ��ó�� ��ܳ���.

Mixed inhibition takes place when both the inhibitor and the substrate are able to bind to the enzyme causing an allosteric effect, in which the inhibitor changes the shape of the active site causing the substrate to be attached to the allosteric site rather than the original, which will cause a completely different reaction.

Mixed inibition: ����� ��ff�� ȥ����8�μ�, �˷ν��׸��� ȿ�� �ҷ���8°ï¿½ï¿½, °ï¿½ï¿½ï¿½ï¿½'�� ���; ������� ������ ��� ��� ��'�� �����°ï¿½ ��8�ν�, ���� �ٸ� ȭ�й���; ��8Ų��.

Substrate and product inhibition is a special case in which either the substrate or the product of enzyme reaction inhibits the enzyme��s activity.

Ư���� ��쿡��, ������ ȭ�й���; ��8�� ���� �λ°ï¿½ï¿½ ��ff ����; �ϴ� ��쵵 �ִ�.

Nonspecific inhibition functions the same way for any type of enzyme.

��Ưd ��ff�� � ~���� ȿ�ҿ͵� ��: ����; ��8Ų��.

For nonspecific inhibition the reaction rate increases proportionally with the temperature until it reaches the optimal rate, the maximum rate it can reach.

��Ưd ��ff�� �µï¿½ï¿½ï¿½ ���Կ� ��� ȭ�к�ȭ�� �׿� ����°ï¿½ �Ͼ�°ï¿½, �ִ�ġ���� �ö°ï¿½, �ٽ� �����ϱ� �����Ѵ�.

At high temperature the protein part of the enzyme will begin to denature, thus inhibiting the reaction.

�µï¿½ï¿½ï¿½ ����ϸ� ȿ���� �ܹ��� �κ��� �����Ͽ�, ȭ�й����� ��ff�� �ۿ��°ï¿½ �ȴ�.

The same applies to pH, the rate of reaction as the pH increases until it reaches a point where it will no longer increase.

pH���� �µï¿½ï¿½ï¿½ ���� ��ȭ�� �����8�� ���ϴ°ï¿½ �ִ�ġ�� ���ϸ� �� �̻� �ö��� �ʴ´ï¿½.

The first step in inventing a new drug starts from the discovery of a new enzyme inhibitor.

��ο� ��°; �����ϱ� '�� ù��=: ȿ�� ��ff�� �°ï¿½ï¿½Ï´ï¿½ ���̴�.

Previously, the only method of doing this was to go through trial-and-error, however nowadays, with the progress of technology, using a rational dug design, it has become possible to predict the shape of substrate and inhibitor would actually fir the enzyme by observing the shape of the active site.

����� ������8� ���ľ��� ��������, ������ �ߴ޷� ����� ȿ�Һ�'�� ���; ������8�ν� ����� ��ff�� ������ ������ �� �°ï¿½ �Ǿ��.

With such things becoming possible, it is no surprise that the use of enzyme inhibitors in the field of pharmacology and biochemistry has increased.

�̷��� ��ǵ�; ~���� �� ��, �ฮ�°ï¿½ ��ȭ�� ���� �� ȿ�� ��f���� ������ �þî³­ �� �׸� ��� ���� �ƴϴ�.

With the gain of popularity as a topic of research, other than the use from drug discovery, inhibitors have come in use for various purposes such as chemotherapy in genetics, metabolic control, pesticides and herbicides, and also as natural poison.

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