Structural basis of enzyme activity regulation by the propeptide of l-lysine α-oxidase precursor from
Crystal structure
L-Lysine α-oxidase
LAAO, l-amino acid oxidase
LysOX, l-lysine α-oxidase
Precursor
Substrate recognition
Journal
Journal of structural biology: X
ISSN: 2590-1524
Titre abrégé: J Struct Biol X
Pays: United States
ID NLM: 101761384
Informations de publication
Date de publication:
2021
2021
Historique:
received:
14
10
2020
revised:
17
12
2020
accepted:
07
01
2021
entrez:
8
2
2021
pubmed:
9
2
2021
medline:
9
2
2021
Statut:
epublish
Résumé
Harmuful proteins are usually synthesized as inactive precursors and are activated by proteolytic processing. l-Amino acid oxidase (LAAO) is a flavoenzyme that catalyzes the oxidative deamination of l-amino acid to produce a 2-oxo acid with ammonia and highly toxic hydrogen peroxide and, therefore, is expressed as a precursor. The LAAO precursor shows significant variation in size and the cleavage pattern for activation. However, the molecular mechanism of how the propeptide suppresses the enzyme activity remains unclear except for deaminating/decarboxylating
Identifiants
pubmed: 33554108
doi: 10.1016/j.yjsbx.2021.100044
pii: S2590-1524(21)00001-5
pmc: PMC7844570
doi:
Types de publication
Journal Article
Langues
eng
Pagination
100044Informations de copyright
© 2021 The Author(s).
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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