# Evaluating potential impact of monoamine oxidase A missense L32S on the function of the enzyme monoamine oxidase A using in silico prediction tools and molecular modeling

## TL;DR

This study examines how a specific genetic change in the MAOA enzyme might contribute to ADHD by using computational tools and modeling.

## Contribution

The study provides new evidence for the pathogenicity of the L32S missense variant in monoamine oxidase A.

## Key findings

- In silico tools suggest the L32S variant is pathogenic.
- Molecular dynamics modeling supports functional impact of the L32S mutation.
- The variant affects the FAD-binding domain of monoamine oxidase A.

## Abstract

Attention-deficit hyperactivity disorder (ADHD) is a neurodevelopmental disorder that affects 6-7% of people worldwide (Wilcutt, 2012). MAOA is a gene that encodes monoamine oxidase A, an enzyme responsible for the regulation and metabolism of monoamines thought to be associated with ADHD. This study investigates a leucine to serine swap at amino acid position 32 in FAD-binding domain of the enzyme monoamine oxidase A. Results from
in silico
prediction tools and molecular dynamics modeling provide evidence to support pathogenicity of the L32S missense variant of monoamine oxidase A.