Why does the Y326I mutant of monoamine oxidase B decompose an endogenous amphetamine at a slower rate than the wild type enzyme? Reaction step elucidated by multiscale molecular simulations-Reference-Cited by-同舟云学术

Why does the Y326I mutant of monoamine oxidase B decompose an endogenous amphetamine at a slower rate than the wild type enzyme? Reaction step elucidated by multiscale molecular simulations

Published:2018 Issue:6 Volume:20 Page:4181-4188
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Pregeljc Domen¹²³⁴⁵,Jug Urška¹²³⁴,Mavri Janez¹²³⁴,Stare Jernej¹²³⁴^ORCID

Affiliation:

1. Theory Department

2. National Institute of Chemistry

3. Ljubljana

4. Slovenia

5. Gimnazija Vič High School

Abstract

Mutated MAO B enzyme decomposes phenylethylamine at slower rate due to changed interactions in the active site.

Funder

Javna Agencija za Raziskovalno Dejavnost RS

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP07069A

Reference77 articles.

1. Abnormal Behavior Associated with a Point Mutation in the Structural Gene for Monoamine Oxidase A

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5. Monoamine oxidase (MAO) intron 13 polymorphism and platelet MAO-B activity in combat-related posttraumatic stress disorder

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