Amine oxidase

From WikiMD's Wellness Encyclopedia

Amine oxidase is a class of enzymes that catalyze the oxidation of amines. They are involved in the metabolism of various biogenic amines, including neurotransmitters, histamine, and trace amines. Amine oxidases play a crucial role in maintaining cellular and physiological homeostasis. There are two main types of amine oxidases: copper-containing amine oxidases (CuAOs) and flavin-containing amine oxidases (FMOs or MAOs, for monoamine oxidases).

Types of Amine Oxidases[edit | edit source]

Copper-Containing Amine Oxidases (CuAOs)[edit | edit source]

CuAOs are widely distributed in plants, bacteria, and animals. They contain copper as a cofactor and typically oxidize primary amines to the corresponding aldehydes, releasing ammonia and hydrogen peroxide. In mammals, CuAOs are involved in the metabolism of dietary and endogenous amines, the regulation of polyamine levels, and the modulation of vascular adhesion and tissue maturation.

Flavin-Containing Amine Oxidases (FMOs or MAOs)[edit | edit source]

FMOs, also known as monoamine oxidases (MAOs), are found in most mammalian tissues and are integral to the mitochondrial outer membrane. They use flavin adenine dinucleotide (FAD) as a cofactor to catalyze the oxidative deamination of monoamines. MAOs play a critical role in the catabolism of neurotransmitters such as serotonin, norepinephrine, and dopamine, thereby regulating mood, arousal, and blood pressure. There are two isoforms of MAO: MAO-A and MAO-B, which differ in their substrate specificity and tissue distribution.

Function[edit | edit source]

Amine oxidases are essential for the detoxification of amines and the regulation of their levels in the body. By metabolizing biogenic amines, these enzymes help to regulate physiological functions such as mood, emotional responses, and blood pressure. In addition, the hydrogen peroxide produced as a byproduct of amine oxidation can serve as a signaling molecule or, in higher concentrations, contribute to oxidative stress and tissue damage.

Clinical Significance[edit | edit source]

Alterations in the activity or expression of amine oxidases have been implicated in various diseases and conditions. For example, abnormal MAO activity has been associated with psychiatric disorders such as depression and anxiety, as well as neurodegenerative diseases like Parkinson's and Alzheimer's disease. Inhibitors of MAO, known as MAO inhibitors (MAOIs), are used as antidepressants and in the treatment of Parkinson's disease.

Copper-containing amine oxidases have been studied for their role in diabetes, obesity, and cardiovascular diseases. The modulation of CuAO activity is considered a potential therapeutic strategy for these conditions.

Research[edit | edit source]

Research on amine oxidases continues to uncover their complex roles in health and disease. Studies are focused on understanding the detailed mechanisms of action, substrate specificity, and regulation of these enzymes. Additionally, the development of selective inhibitors or activators of amine oxidases holds promise for therapeutic applications in various diseases.

WikiMD
Navigation: Wellness - Encyclopedia - Health topics - Disease Index‏‎ - Drugs - World Directory - Gray's Anatomy - Keto diet - Recipes

Search WikiMD

Ad.Tired of being Overweight? Try W8MD's physician weight loss program.
Semaglutide (Ozempic / Wegovy and Tirzepatide (Mounjaro / Zepbound) available.
Advertise on WikiMD

WikiMD's Wellness Encyclopedia

Let Food Be Thy Medicine
Medicine Thy Food - Hippocrates

Medical Disclaimer: WikiMD is not a substitute for professional medical advice. The information on WikiMD is provided as an information resource only, may be incorrect, outdated or misleading, and is not to be used or relied on for any diagnostic or treatment purposes. Please consult your health care provider before making any healthcare decisions or for guidance about a specific medical condition. WikiMD expressly disclaims responsibility, and shall have no liability, for any damages, loss, injury, or liability whatsoever suffered as a result of your reliance on the information contained in this site. By visiting this site you agree to the foregoing terms and conditions, which may from time to time be changed or supplemented by WikiMD. If you do not agree to the foregoing terms and conditions, you should not enter or use this site. See full disclaimer.
Credits:Most images are courtesy of Wikimedia commons, and templates Wikipedia, licensed under CC BY SA or similar.

Contributors: Prab R. Tumpati, MD