Architecture Insight of Bifidobacterial α-L-Fucosidases
This article belongs to the Special Issue Frontiers in Protein Structure Research
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Multidisciplinary Digital Publishing Institute
2021-08-06
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| Subjects: | Bifidobacteria, Glycosyl hydrolases, Fucosidases, Conserved domains, Human milk, |
| Online Access: | http://hdl.handle.net/10261/265835 http://dx.doi.org/10.13039/501100004837 https://api.elsevier.com/content/abstract/scopus_id/85111901990 |
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dig-inia-es-10261-2658352024-10-26T21:17:51Z Architecture Insight of Bifidobacterial α-L-Fucosidases Curiel, José Antonio Peirotén, Ángela Landete, José María Ruiz de la Bastida, Ana Langa, Susana Arques Orobón, Juan Luis Ministerio de Ciencia e Innovación (España) Curiel, J.A. [0000-0002-0111-1437] Peirotén, Ángela [0000-0002-1532-8530] Landete, José María [0000-0002-5147-3989] De la Bastida, A.R. [0000-0002-0650-7326] Langa, S. [0000-0003-2729-219X] Arques, J.L. [0000-0002-8548-0183] Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72] Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk This article belongs to the Special Issue Frontiers in Protein Structure Research 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, alpha-L-fucosidases play a key role in this successful bifidobacterial colonization allowing the utilization of these substrates. Although a considerable number of alpha-L-fucosidases from bifidobacteria have been identified by computational analysis, only a few of them have been characterized. Hitherto, alpha-L-fucosidases are classified into three families: GH29, GH95, and GH151, based on their catalytic structure. However, bifidobacterial alpha-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 alpha-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, Bifidobacterium longum subsp. infantis species exhibited the greatest number of phylogenetic lineages in their fucosidases clustered in every family: GH29, GH95, and GH151. Since alpha-L-fucosidases phylogenetically descended from other glycosyl hydrolase families, we hypothesized that they could exhibit additional glycosidase activities other than fucosidase, raising the possibility of their application to transfucosylate substrates other than lactose in order to synthesis novel prebiotics. This research was funded by Spanish Ministry of Science and Innovation—Ramón y Cajal program, grant number RYC2019-026368-I. Peer reviewed 2022-03-31T08:13:14Z 2022-03-31T08:13:14Z 2021-08-06 artículo http://purl.org/coar/resource_type/c_6501 International Journal of Molecular Sciences 22 (16): 8462 (2021) http://hdl.handle.net/10261/265835 10.3390/ijms22168462 1422-0067 http://dx.doi.org/10.13039/501100004837 2-s2.0-85111901990 https://api.elsevier.com/content/abstract/scopus_id/85111901990 en #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/Ministerio de Ciencia e Innovación//RYC2019-026368-I International journal of molecular sciences Publisher's version https://doi.org/10.3390/ijms22168462 Sí open Multidisciplinary Digital Publishing Institute |
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Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk |
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Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk Curiel, José Antonio Peirotén, Ángela Landete, José María Ruiz de la Bastida, Ana Langa, Susana Arques Orobón, Juan Luis Architecture Insight of Bifidobacterial α-L-Fucosidases |
| description |
This article belongs to the Special Issue Frontiers in Protein Structure Research |
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Ministerio de Ciencia e Innovación (España) |
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Ministerio de Ciencia e Innovación (España) Curiel, José Antonio Peirotén, Ángela Landete, José María Ruiz de la Bastida, Ana Langa, Susana Arques Orobón, Juan Luis |
| format |
artículo |
| topic_facet |
Bifidobacteria Glycosyl hydrolases Fucosidases Conserved domains Human milk |
| author |
Curiel, José Antonio Peirotén, Ángela Landete, José María Ruiz de la Bastida, Ana Langa, Susana Arques Orobón, Juan Luis |
| author_sort |
Curiel, José Antonio |
| title |
Architecture Insight of Bifidobacterial α-L-Fucosidases |
| title_short |
Architecture Insight of Bifidobacterial α-L-Fucosidases |
| title_full |
Architecture Insight of Bifidobacterial α-L-Fucosidases |
| title_fullStr |
Architecture Insight of Bifidobacterial α-L-Fucosidases |
| title_full_unstemmed |
Architecture Insight of Bifidobacterial α-L-Fucosidases |
| title_sort |
architecture insight of bifidobacterial α-l-fucosidases |
| publisher |
Multidisciplinary Digital Publishing Institute |
| publishDate |
2021-08-06 |
| url |
http://hdl.handle.net/10261/265835 http://dx.doi.org/10.13039/501100004837 https://api.elsevier.com/content/abstract/scopus_id/85111901990 |
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1816136059003600896 |