ADH-1: Difference between revisions

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{{Short description|Overview of ADH-1, a chemical compound}}
== Alcohol Dehydrogenase 1 (ADH-1) ==
{{DISPLAYTITLE:ADH-1}}


==Overview==
[[File:ADH-1.svg|thumb|right|Diagram of Alcohol Dehydrogenase 1]]
'''ADH-1''' is a chemical compound that has been studied for its potential therapeutic applications, particularly in the context of cancer treatment. It is known to inhibit the function of certain proteins involved in cell adhesion, which can play a role in the spread of cancer cells.


==Mechanism of Action==
'''Alcohol Dehydrogenase 1''' ('''ADH-1''') is an enzyme that plays a crucial role in the metabolism of alcohols within the human body. It is part of the [[alcohol dehydrogenase]] family, which is responsible for the oxidation of alcohols to aldehydes and ketones. ADH-1 is primarily found in the [[liver]], where it catalyzes the conversion of [[ethanol]] to [[acetaldehyde]], a key step in the metabolic pathway of alcohol.
ADH-1 functions primarily as an inhibitor of [[N-cadherin]], a protein that is involved in the adhesion of cells to one another. By inhibiting N-cadherin, ADH-1 can disrupt the interactions between cancer cells and their surrounding environment, potentially reducing the ability of cancer cells to metastasize.


==Clinical Applications==
== Structure ==
Research into ADH-1 has focused on its use as a potential treatment for various types of cancer. The compound has been investigated in clinical trials to assess its efficacy and safety in combination with other cancer therapies. The ability of ADH-1 to enhance the effects of chemotherapy and radiation therapy is of particular interest.


==Chemical Properties==
ADH-1 is a [[zinc]]-dependent enzyme, meaning it requires zinc ions to function properly. The enzyme is a dimer, consisting of two identical subunits. Each subunit contains a zinc ion that is essential for its catalytic activity. The structure of ADH-1 allows it to bind to alcohol molecules and facilitate their conversion to aldehydes.
ADH-1 is a small molecule with specific chemical properties that allow it to interact with target proteins in the body. Its structure enables it to bind effectively to N-cadherin, thereby inhibiting its function.


==Research and Development==
== Function ==
The development of ADH-1 has involved extensive research to understand its pharmacokinetics, pharmacodynamics, and potential side effects. Ongoing studies aim to optimize its use in clinical settings and to explore its effectiveness in combination with other therapeutic agents.


==Related pages==
The primary function of ADH-1 is to metabolize ethanol, the type of alcohol found in alcoholic beverages. When ethanol is consumed, ADH-1 oxidizes it to acetaldehyde, which is then further metabolized by [[aldehyde dehydrogenase]] to [[acetic acid]]. This process is crucial for the detoxification of alcohol in the body.
* [[N-cadherin]]
* [[Cancer treatment]]
* [[Metastasis]]
* [[Chemotherapy]]


==Gallery==
== Genetic Variability ==
<gallery>
File:ADH-1.svg|Structure of ADH-1
</gallery>


[[Category:Chemical compounds]]
There is significant genetic variability in the ADH-1 gene among different populations. This variability can affect the enzyme's activity and, consequently, an individual's ability to metabolize alcohol. Some variants of ADH-1 are associated with faster or slower metabolism of ethanol, which can influence susceptibility to [[alcohol use disorder]] and other alcohol-related health issues.
[[Category:Cancer treatments]]
 
== Clinical Significance ==
 
ADH-1 is of clinical interest due to its role in alcohol metabolism. Variations in the ADH-1 gene can lead to differences in alcohol tolerance and the risk of developing alcohol-related diseases. Understanding these genetic differences can help in the development of personalized medical approaches to treating alcohol use disorders.
 
== Related Enzymes ==
 
ADH-1 is one of several alcohol dehydrogenases in humans. Other members of the family include ADH-2 and ADH-3, which also participate in alcohol metabolism but have different substrate specificities and tissue distributions.
 
== Related Pages ==
 
* [[Alcohol dehydrogenase]]
* [[Ethanol metabolism]]
* [[Aldehyde dehydrogenase]]
* [[Alcohol use disorder]]
 
[[Category:Enzymes]]
[[Category:Metabolism]]
[[Category:Alcohol]]

Latest revision as of 03:26, 13 February 2025

Alcohol Dehydrogenase 1 (ADH-1)[edit]

Diagram of Alcohol Dehydrogenase 1

Alcohol Dehydrogenase 1 (ADH-1) is an enzyme that plays a crucial role in the metabolism of alcohols within the human body. It is part of the alcohol dehydrogenase family, which is responsible for the oxidation of alcohols to aldehydes and ketones. ADH-1 is primarily found in the liver, where it catalyzes the conversion of ethanol to acetaldehyde, a key step in the metabolic pathway of alcohol.

Structure[edit]

ADH-1 is a zinc-dependent enzyme, meaning it requires zinc ions to function properly. The enzyme is a dimer, consisting of two identical subunits. Each subunit contains a zinc ion that is essential for its catalytic activity. The structure of ADH-1 allows it to bind to alcohol molecules and facilitate their conversion to aldehydes.

Function[edit]

The primary function of ADH-1 is to metabolize ethanol, the type of alcohol found in alcoholic beverages. When ethanol is consumed, ADH-1 oxidizes it to acetaldehyde, which is then further metabolized by aldehyde dehydrogenase to acetic acid. This process is crucial for the detoxification of alcohol in the body.

Genetic Variability[edit]

There is significant genetic variability in the ADH-1 gene among different populations. This variability can affect the enzyme's activity and, consequently, an individual's ability to metabolize alcohol. Some variants of ADH-1 are associated with faster or slower metabolism of ethanol, which can influence susceptibility to alcohol use disorder and other alcohol-related health issues.

Clinical Significance[edit]

ADH-1 is of clinical interest due to its role in alcohol metabolism. Variations in the ADH-1 gene can lead to differences in alcohol tolerance and the risk of developing alcohol-related diseases. Understanding these genetic differences can help in the development of personalized medical approaches to treating alcohol use disorders.

Related Enzymes[edit]

ADH-1 is one of several alcohol dehydrogenases in humans. Other members of the family include ADH-2 and ADH-3, which also participate in alcohol metabolism but have different substrate specificities and tissue distributions.

Related Pages[edit]