Architecture Insight of Bifidobacterial α-L-Fucosidases.
bifidobacteria
conserved domains
fucosidases
glycosyl hydrolases
human milk
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
06 Aug 2021
06 Aug 2021
Historique:
received:
29
06
2021
revised:
03
08
2021
accepted:
04
08
2021
entrez:
27
8
2021
pubmed:
28
8
2021
medline:
21
9
2021
Statut:
epublish
Résumé
Fucosylated carbohydrates and glycoproteins from human breast milk are essential for the development of the gut microbiota in early life because they are selectively metabolized by bifidobacteria. In this regard, α-L-fucosidases play a key role in this successful bifidobacterial colonization allowing the utilization of these substrates. Although a considerable number of α-L-fucosidases from bifidobacteria have been identified by computational analysis, only a few of them have been characterized. Hitherto, α-L-fucosidases are classified into three families: GH29, GH95, and GH151, based on their catalytic structure. However, bifidobacterial α-L-fucosidases belonging to a particular family show significant differences in their sequence. Because this fact could underlie distinct phylogenetic evolution, here extensive similarity searches and comparative analyses of the bifidobacterial α-L-fucosidases identified were carried out with the assistance of previous physicochemical studies available. This work reveals four and two paralogue bifidobacterial fucosidase groups within GH29 and GH95 families, respectively. Moreover,
Identifiants
pubmed: 34445166
pii: ijms22168462
doi: 10.3390/ijms22168462
pmc: PMC8395109
pii:
doi:
Substances chimiques
Bacterial Proteins
0
Fucose
28RYY2IV3F
alpha-L-Fucosidase
EC 3.2.1.51
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministerio de Ciencia e Innovación
ID : RYC2019-026368-I
Organisme : Ministerio de Ciencia e Innovación
ID : PRE2018-086293
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