Aldehyde oxidase: Difference between revisions

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{{Short description|An enzyme involved in the metabolism of aldehydes and nitrogen-containing compounds}}
{{Short description|An enzyme involved in the metabolism of aldehydes and nitrogen-containing compounds}}
{{Enzyme}}
{{Use dmy dates|date=October 2023}}


'''Aldehyde oxidase''' is a [[molybdenum]]-containing enzyme that plays a crucial role in the metabolism of [[aldehydes]] and [[nitrogen]]-containing compounds. It is involved in the oxidation of aldehydes to [[carboxylic acids]] and the hydroxylation of heterocycles. Aldehyde oxidase is found in the [[cytosol]] of cells and is particularly abundant in the [[liver]].
==Aldehyde Oxidase==
[[File:Aldehydoxidase.png|thumb|right|Diagram of Aldehyde Oxidase]]
'''Aldehyde oxidase''' is a [[molybdenum]]-containing enzyme that plays a crucial role in the metabolism of a wide range of endogenous and exogenous [[aldehydes]] and [[nitrogen]]-containing compounds. It is a member of the [[xanthine oxidase]] family of enzymes and is found in many tissues throughout the body, including the [[liver]], [[lung]], and [[kidney]].


==Structure==
==Structure==
Aldehyde oxidase is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains a molybdenum cofactor, two iron-sulfur clusters, and a flavin adenine dinucleotide (FAD) moiety. The molybdenum cofactor is essential for the enzyme's catalytic activity, facilitating the transfer of oxygen to the substrate.
Aldehyde oxidase is a complex enzyme that contains a molybdenum cofactor, two iron-sulfur clusters, and a flavin adenine dinucleotide (FAD) moiety. The enzyme is a homodimer, meaning it consists of two identical subunits. Each subunit contains the necessary cofactors for catalytic activity.


==Function==
==Function==
The primary function of aldehyde oxidase is to catalyze the oxidation of aldehydes to carboxylic acids. This reaction involves the transfer of electrons from the aldehyde to molecular oxygen, producing the corresponding carboxylic acid and hydrogen peroxide. Aldehyde oxidase also participates in the metabolism of various drugs and xenobiotics, contributing to their detoxification and elimination from the body.
The primary function of aldehyde oxidase is to catalyze the oxidation of aldehydes to their corresponding [[carboxylic acids]]. This reaction involves the transfer of electrons from the aldehyde to molecular [[oxygen]], producing the carboxylic acid and [[hydrogen peroxide]] as byproducts. Aldehyde oxidase also participates in the metabolism of various [[drugs]] and [[xenobiotics]], contributing to their detoxification and elimination from the body.
 
==Substrate Specificity==
Aldehyde oxidase exhibits broad substrate specificity, acting on a wide range of aldehydes and nitrogen-containing heterocycles. It is known to oxidize aromatic and aliphatic aldehydes, as well as purines, pyrimidines, and pteridines. This broad substrate range makes aldehyde oxidase an important enzyme in drug metabolism, as it can influence the pharmacokinetics and pharmacodynamics of various therapeutic agents.


==Clinical Significance==
==Clinical Significance==
Aldehyde oxidase is involved in the metabolism of several clinically important drugs, including [[methotrexate]], [[famciclovir]], and [[ziprasidone]]. Variations in aldehyde oxidase activity can lead to differences in drug metabolism and response among individuals. Genetic polymorphisms in the aldehyde oxidase gene can result in altered enzyme activity, affecting drug efficacy and toxicity.
Aldehyde oxidase is involved in the metabolism of several clinically important drugs, including [[antidepressants]], [[antipsychotics]], and [[antiparasitic]] agents. Variations in aldehyde oxidase activity can affect drug metabolism and lead to differences in drug efficacy and toxicity among individuals. Genetic polymorphisms in the gene encoding aldehyde oxidase can result in altered enzyme activity, impacting drug metabolism.


==Related Enzymes==
==Related Enzymes==
Aldehyde oxidase is part of the [[xanthine oxidase]] family of enzymes, which also includes [[xanthine dehydrogenase]] and [[xanthine oxidoreductase]]. These enzymes share structural similarities and catalytic mechanisms, but differ in their substrate specificities and physiological roles.
Aldehyde oxidase is closely related to other molybdenum-containing enzymes, such as [[xanthine oxidase]] and [[sulfite oxidase]]. These enzymes share structural similarities and have overlapping substrate specificities, although each enzyme has distinct physiological roles.


==Gallery==
==Research and Applications==
<gallery>
Research on aldehyde oxidase has focused on its role in drug metabolism and its potential as a target for drug development. Inhibitors of aldehyde oxidase are being investigated for their ability to modulate drug metabolism and improve the pharmacokinetic properties of therapeutic agents.
File:Aldehydoxidase.png|Structure of aldehyde oxidase
</gallery>


==Related pages==
==Related pages==
* [[Xanthine oxidase]]
* [[Xanthine oxidase]]
* [[Molybdenum cofactor]]
* [[Drug metabolism]]
* [[Drug metabolism]]
* [[Molybdenum cofactor]]
* [[Enzyme kinetics]]


[[Category:Enzymes]]
[[Category:Enzymes]]
[[Category:Oxidoreductases]]
[[Category:Drug metabolism]]
[[Category:Drug metabolism]]
[[Category:Oxidoreductases]]

Latest revision as of 11:36, 15 February 2025

An enzyme involved in the metabolism of aldehydes and nitrogen-containing compounds



Aldehyde Oxidase[edit]

Diagram of Aldehyde Oxidase

Aldehyde oxidase is a molybdenum-containing enzyme that plays a crucial role in the metabolism of a wide range of endogenous and exogenous aldehydes and nitrogen-containing compounds. It is a member of the xanthine oxidase family of enzymes and is found in many tissues throughout the body, including the liver, lung, and kidney.

Structure[edit]

Aldehyde oxidase is a complex enzyme that contains a molybdenum cofactor, two iron-sulfur clusters, and a flavin adenine dinucleotide (FAD) moiety. The enzyme is a homodimer, meaning it consists of two identical subunits. Each subunit contains the necessary cofactors for catalytic activity.

Function[edit]

The primary function of aldehyde oxidase is to catalyze the oxidation of aldehydes to their corresponding carboxylic acids. This reaction involves the transfer of electrons from the aldehyde to molecular oxygen, producing the carboxylic acid and hydrogen peroxide as byproducts. Aldehyde oxidase also participates in the metabolism of various drugs and xenobiotics, contributing to their detoxification and elimination from the body.

Clinical Significance[edit]

Aldehyde oxidase is involved in the metabolism of several clinically important drugs, including antidepressants, antipsychotics, and antiparasitic agents. Variations in aldehyde oxidase activity can affect drug metabolism and lead to differences in drug efficacy and toxicity among individuals. Genetic polymorphisms in the gene encoding aldehyde oxidase can result in altered enzyme activity, impacting drug metabolism.

Related Enzymes[edit]

Aldehyde oxidase is closely related to other molybdenum-containing enzymes, such as xanthine oxidase and sulfite oxidase. These enzymes share structural similarities and have overlapping substrate specificities, although each enzyme has distinct physiological roles.

Research and Applications[edit]

Research on aldehyde oxidase has focused on its role in drug metabolism and its potential as a target for drug development. Inhibitors of aldehyde oxidase are being investigated for their ability to modulate drug metabolism and improve the pharmacokinetic properties of therapeutic agents.

Related pages[edit]