Origins of peptidases.
Asparagine peptide lyase
Evolution
Horizontal gene transfer
Last universal common ancestor
Peptidase
Proteolytic enzyme
Journal
Biochimie
ISSN: 1638-6183
Titre abrégé: Biochimie
Pays: France
ID NLM: 1264604
Informations de publication
Date de publication:
Nov 2019
Nov 2019
Historique:
received:
07
03
2019
accepted:
29
07
2019
pubmed:
5
8
2019
medline:
31
12
2019
entrez:
5
8
2019
Statut:
ppublish
Résumé
The distribution of all peptidase homologues across all phyla of organisms was analysed to determine within which kingdom each of the 271 families originated. No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methionyl aminopeptides are missing from some clades. There are 33 peptidase families common to archaea, bacteria and eukaryotes and are assumed to have originated in the last universal common ancestor (LUCA). These include peptidases with different catalytic types, exo- and endopeptidases, peptidases with different tertiary structures and peptidases from different families but with similar structures. This implies that the different catalytic types and structures pre-date LUCA. Other families have had their origins in the ancestors of viruses, archaea, bacteria, fungi, plants and animals, and a number of families have had their origins in the ancestors of particular phyla. The evolution of peptidases is compared to recent hypotheses about the evolution of organisms.
Identifiants
pubmed: 31377195
pii: S0300-9084(19)30226-3
doi: 10.1016/j.biochi.2019.07.026
pmc: PMC7117030
pii:
doi:
Substances chimiques
Peptide Hydrolases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
4-18Informations de copyright
Copyright © 2019 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.
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