Current trends in the structure-activity relationships of sialyltransferases
| Autor: | Anne Harduin-Lepers, Anne Imberty, Christelle Breton, Charlotte Jeanneau, Philippe Delannoy, Magali Audry |
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| Přispěvatelé: | inconnu, Inconnu, Centre de Recherches sur les Macromolécules Végétales (CERMAV), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 (UGSF), Institut National de la Recherche Agronomique (INRA)-Université de Lille-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), Université Lille Nord de France (COMUE), Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 (UGSF), Université de Lille-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF), Université Joseph Fourier - Grenoble 1 (UJF)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Université de Lille-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Models
Molecular Protein Folding CAZy [SDV.BIO]Life Sciences [q-bio]/Biotechnology MESH: Protein Folding MESH: Sialyltransferases Virulence [SDV.CAN]Life Sciences [q-bio]/Cancer [SDV.BID.SPT]Life Sciences [q-bio]/Biodiversity/Systematics Phylogenetics and taxonomy Biochemistry Structure-Activity Relationship 03 medical and health sciences chemistry.chemical_compound MESH: Structure-Activity Relationship [SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN] Glycosyltransferase Animals Humans MESH: Animals [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Histidine ComputingMilieux_MISCELLANEOUS 030304 developmental biology chemistry.chemical_classification 0303 health sciences MESH: Humans biology [SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE] 030302 biochemistry & molecular biology Active site Cytidine [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology [SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular Networks [q-bio.MN] [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM] N-Acetylneuraminic Acid Sialyltransferases [SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Enzyme chemistry Biocatalysis biology.protein Protein folding MESH: N-Acetylneuraminic Acid MESH: Biocatalysis MESH: Models Molecular |
| Zdroj: | Glycobiology Glycobiology, Oxford University Press (OUP), 2011, 21 (6), pp.716-726. ⟨10.1093/glycob/cwq189⟩ Glycobiology, Oxford University Press (OUP), 2011, 21 (6), pp.716-26 Glycobiology, Oxford University Press (OUP), 2011, pp.716-726 Glycobiology, 2011, 21 (6), pp.716-26 |
| ISSN: | 0959-6658 1460-2423 |
| DOI: | 10.1093/glycob/cwq189⟩ |
| Popis: | International audience; Sialyltransferases (STs) represent an important group of enzymes that transfer N-acetylneuraminic acid (Neu5Ac) from cytidine monophosphate-Neu5Ac to various acceptor substrates. In higher animals, sialylated oligosaccharide structures play crucial roles in many biological processes but also in diseases, notably in microbial infection and cancer. Cell surface sialic acids have also been found in a few microorganisms, mainly pathogenic bacteria, and their presence is often associated with virulence. STs are distributed into five different families in the CAZy database (http://www.cazy.org/). On the basis of crystallographic data available for three ST families and fold recognition analysis for the two other families, STs can be grouped into two structural superfamilies that represent variations of the canonical glycosyltransferase (GT-A and GT-B) folds. These two superfamilies differ in the nature of their active site residues, notably the catalytic base (a histidine or an aspartate residue). The observed structural and functional differences strongly suggest that these two structural superfamilies have evolved independently. |
| Databáze: | OpenAIRE |
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