Arylalkalamine N-acetyltransferase-1 acts on a secondary amine in the yellow fever mosquito, Aedes aegypti.
N-acetyltransferase
epinephrine
functional analysis
haemostasis
mosquito
novel substrate
Journal
FEBS letters
ISSN: 1873-3468
Titre abrégé: FEBS Lett
Pays: England
ID NLM: 0155157
Informations de publication
Date de publication:
04 2022
04 2022
Historique:
revised:
06
02
2022
received:
27
12
2021
accepted:
09
02
2022
pubmed:
19
2
2022
medline:
28
4
2022
entrez:
18
2
2022
Statut:
ppublish
Résumé
Arylalkylamine N-acetyltransferase (aaNAT) in Aedes aegypti is primarily involved in cuticle pigmentation and formation. The reported arylalkylamine substrates are all primary amines. In this study, we report a novel substrate, a secondary amine, of Ae. aegypti aaNAT1. The recombinant aaNAT1 protein exhibited high activity to a secondary amine, epinephrine, which has not been reported for any aaNATs previously. Structure-activity relationship study demonstrated that aaNAT1 has an epinephrine-binding site, and molecular docking and dynamic simulation showed that epinephrine is quite stable in the active cavity. Further functional studies demonstrated that epinephrine affected mosquito fecundity, egg hatching and development. The new biochemical function of aaNAT1 in metabolizing epinephrine could reduce some negative effects of the compound in the mosquito.
Identifiants
pubmed: 35178730
doi: 10.1002/1873-3468.14316
doi:
Substances chimiques
Amines
0
Isoenzymes
0
Recombinant Proteins
0
Acetyltransferases
EC 2.3.1.-
Arylamine N-Acetyltransferase
EC 2.3.1.5
N-acetyltransferase 1
EC 2.3.1.5
Epinephrine
YKH834O4BH
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1081-1091Informations de copyright
© 2022 Federation of European Biochemical Societies.
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