The Dual α-Amidation System in Scorpion Venom Glands.
amidation
evolution
posttranslational modifications
scorpion
transcriptomics
Journal
Toxins
ISSN: 2072-6651
Titre abrégé: Toxins (Basel)
Pays: Switzerland
ID NLM: 101530765
Informations de publication
Date de publication:
20 07 2019
20 07 2019
Historique:
received:
04
06
2019
revised:
18
07
2019
accepted:
18
07
2019
entrez:
24
7
2019
pubmed:
25
7
2019
medline:
1
9
2020
Statut:
epublish
Résumé
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 (PHM
Identifiants
pubmed: 31330798
pii: toxins11070425
doi: 10.3390/toxins11070425
pmc: PMC6669573
pii:
doi:
Substances chimiques
Multienzyme Complexes
0
Scorpion Venoms
0
Mixed Function Oxygenases
EC 1.-
peptidylglycine monooxygenase
EC 1.14.17.3
Carboxypeptidase H
EC 3.4.17.10
Proprotein Convertases
EC 3.4.21.-
Amidine-Lyases
EC 4.3.2.-
peptidylamidoglycolate lyase
EC 4.3.2.5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
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