Document Type
Article
Publication Date
11-1-2020
Publication Title
Medical Hypotheses
Keywords
Alamandine, Aspartate β-decarboxylase, Gut bacteria, Renin-angiotensin system
ISSN
0306-9877
Volume
144
First Page
110038
Abstract
The understanding of the renin-angiotensin system (RAS) has significantly expanded over the last two decades. The elucidation of angiotensin-converting enzyme 2 (ACE2) that converts angiotensin (Ang) II into Ang (1-7) led to the discovery of the cardio-protective axis of the RAS. In addition, novel components of the system, Angiotensin A (Ang A) and alamandine have been identified. Like Ang (1-7), alamandine is a vasodilator and can counteract the effects of Ang II by increasing nitric oxide release from the endothelium and decreasing nicotinamide adenine dinucleotide phosphate oxidase (NADPH)-related superoxide production. Theoretically, alamandine can be derived from Ang (1-7) by decarboxylation of the N-terminal aspartic acid residue to alanine, but the enzyme responsible for this is still unknown. To date, no human or mammalian enzyme with the assigned decarboxylase activity has been identified. However, several bacterial enzymes capable of converting aspartate to alanine have been reported. Therefore, we hypothesize that a bacterial enzyme, most likely present in the microbiome of the gastrointestinal tract, the heart, or systemic circulation could metabolize Ang II, and/or Ang 1-7, to Ang A and alamandine, respectively, in mammals.
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
NSUWorks Citation
Jha, Shalinee; Speth, Robert C.; and Macheroux, Peter, "The possible role of a bacterial aspartate β-decarboxylase in the biosynthesis of alamandine" (2020). HPD Articles. 52.
https://nsuworks.nova.edu/hpd_facarticles/52
ORCID ID
0000-0002-6434-2143
DOI
10.1016/j.mehy.2020.110038
Copyright
Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.
