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Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes

Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a dive...

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Autores principales: Kitainda, Vivian, Jez, Joseph M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8468904/
https://www.ncbi.nlm.nih.gov/pubmed/34573132
http://dx.doi.org/10.3390/antiox10091500
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author Kitainda, Vivian
Jez, Joseph M.
author_facet Kitainda, Vivian
Jez, Joseph M.
author_sort Kitainda, Vivian
collection PubMed
description Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a diverse class of natural products. Glucosinolate function stems from their hydrolysis products, which are responsible for the strong flavors of Brassicales plants, such as mustard, and serve as plant defense molecules by repelling insects, fighting fungal infections, and discouraging herbivory. Additionally, certain hydrolysis products such as isothiocyanates can potentially serve as cancer prevention agents in humans. The breadth of glucosinolate function is a result of its great structural diversity, which comes from the use of aliphatic, aromatic and indole amino acids as precursors and elongation of some side chains by up to nine carbons, which, after the formation of the core glucosinolate structure, can undergo further chemical modifications. Aliphatic methionine-derived glucosinolates are the most abundant form of these compounds. Although both elongation and chemical modification of amino acid side chains are important for aliphatic glucosinolate diversity, its elongation process has not been well described at the molecular level. Here, we summarize new insights on the iterative chain-elongation enzymes methylthioalkylmalate synthase (MAMS) and isopropylmalate dehydrogenase (IPMDH).
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spelling pubmed-84689042021-09-27 Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes Kitainda, Vivian Jez, Joseph M. Antioxidants (Basel) Review Plants evolved specialized metabolic pathways through gene duplication and functional divergence of enzymes involved in primary metabolism. The results of this process are varied pathways that produce an array of natural products useful to both plants and humans. In plants, glucosinolates are a diverse class of natural products. Glucosinolate function stems from their hydrolysis products, which are responsible for the strong flavors of Brassicales plants, such as mustard, and serve as plant defense molecules by repelling insects, fighting fungal infections, and discouraging herbivory. Additionally, certain hydrolysis products such as isothiocyanates can potentially serve as cancer prevention agents in humans. The breadth of glucosinolate function is a result of its great structural diversity, which comes from the use of aliphatic, aromatic and indole amino acids as precursors and elongation of some side chains by up to nine carbons, which, after the formation of the core glucosinolate structure, can undergo further chemical modifications. Aliphatic methionine-derived glucosinolates are the most abundant form of these compounds. Although both elongation and chemical modification of amino acid side chains are important for aliphatic glucosinolate diversity, its elongation process has not been well described at the molecular level. Here, we summarize new insights on the iterative chain-elongation enzymes methylthioalkylmalate synthase (MAMS) and isopropylmalate dehydrogenase (IPMDH). MDPI 2021-09-21 /pmc/articles/PMC8468904/ /pubmed/34573132 http://dx.doi.org/10.3390/antiox10091500 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kitainda, Vivian
Jez, Joseph M.
Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title_full Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title_fullStr Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title_full_unstemmed Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title_short Structural Studies of Aliphatic Glucosinolate Chain-Elongation Enzymes
title_sort structural studies of aliphatic glucosinolate chain-elongation enzymes
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8468904/
https://www.ncbi.nlm.nih.gov/pubmed/34573132
http://dx.doi.org/10.3390/antiox10091500
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