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The Dual α-Amidation System in Scorpion Venom Glands

Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion pro...

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Autores principales: Delgado-Prudencio, Gustavo, Possani, Lourival D., Becerril, Baltazar, Ortiz, Ernesto
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669573/
https://www.ncbi.nlm.nih.gov/pubmed/31330798
http://dx.doi.org/10.3390/toxins11070425
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author Delgado-Prudencio, Gustavo
Possani, Lourival D.
Becerril, Baltazar
Ortiz, Ernesto
author_facet Delgado-Prudencio, Gustavo
Possani, Lourival D.
Becerril, Baltazar
Ortiz, Ernesto
author_sort Delgado-Prudencio, Gustavo
collection PubMed
description Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion proproteins suggests that a conserved enzymatic α-amidation system must be responsible for this modification of scorpion peptides. A transcriptomic approach was employed to identify sequences putatively encoding enzymes of the α-amidation pathway. A dual enzymatic α-amidation system was found, consisting of the membrane-anchored, bifunctional, peptidylglycine α-amidating monooxygenase (PAM) and its paralogs, soluble monofunctional peptidylglycine α-hydroxylating monooxygenase (PHMm) and peptidyl-α-hydroxyglycine α-amidating lyase (PALm). Independent genes encode these three enzymes. Amino acid residues responsible for ion coordination and enzymatic activity are conserved in these sequences, suggesting that the enzymes are functional. Potential endoproteolytic recognition sites for proprotein convertases in the PAM sequence indicate that PAM-derived soluble isoforms may also be expressed. Sequences potentially encoding proprotein convertases (PC1 and PC2), carboxypeptidase E (CPE), and other enzymes of the α-amidation pathway, were also found, confirming the presence of this pathway in scorpions.
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spelling pubmed-66695732019-08-08 The Dual α-Amidation System in Scorpion Venom Glands Delgado-Prudencio, Gustavo Possani, Lourival D. Becerril, Baltazar Ortiz, Ernesto Toxins (Basel) Article Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion proproteins suggests that a conserved enzymatic α-amidation system must be responsible for this modification of scorpion peptides. A transcriptomic approach was employed to identify sequences putatively encoding enzymes of the α-amidation pathway. A dual enzymatic α-amidation system was found, consisting of the membrane-anchored, bifunctional, peptidylglycine α-amidating monooxygenase (PAM) and its paralogs, soluble monofunctional peptidylglycine α-hydroxylating monooxygenase (PHMm) and peptidyl-α-hydroxyglycine α-amidating lyase (PALm). Independent genes encode these three enzymes. Amino acid residues responsible for ion coordination and enzymatic activity are conserved in these sequences, suggesting that the enzymes are functional. Potential endoproteolytic recognition sites for proprotein convertases in the PAM sequence indicate that PAM-derived soluble isoforms may also be expressed. Sequences potentially encoding proprotein convertases (PC1 and PC2), carboxypeptidase E (CPE), and other enzymes of the α-amidation pathway, were also found, confirming the presence of this pathway in scorpions. MDPI 2019-07-20 /pmc/articles/PMC6669573/ /pubmed/31330798 http://dx.doi.org/10.3390/toxins11070425 Text en © 2019 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Delgado-Prudencio, Gustavo
Possani, Lourival D.
Becerril, Baltazar
Ortiz, Ernesto
The Dual α-Amidation System in Scorpion Venom Glands
title The Dual α-Amidation System in Scorpion Venom Glands
title_full The Dual α-Amidation System in Scorpion Venom Glands
title_fullStr The Dual α-Amidation System in Scorpion Venom Glands
title_full_unstemmed The Dual α-Amidation System in Scorpion Venom Glands
title_short The Dual α-Amidation System in Scorpion Venom Glands
title_sort dual α-amidation system in scorpion venom glands
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6669573/
https://www.ncbi.nlm.nih.gov/pubmed/31330798
http://dx.doi.org/10.3390/toxins11070425
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