Probing the CMP-Sialic Acid Donor Specificity of Two Human ß-d-Galactoside Sialyltransferases (ST3GalâI and ST6GalâI) Selectively Acting on O- and N-Glycosylproteins.

Noel, Maxence; Gilormini, Pierre-André; Cogez, Virginie; Yamakawa, Nao; Vicogne, Dorothée; Lion, Cédric; Biot, Christophe; Guérardel, Yann; Harduin-Lepers, Anne

Probing the CMP-Sialic Acid Donor Specificity of Two Human ß-d-Galactoside Sialyltransferases (ST3GalâI and ST6GalâI) Selectively Acting on O- and N-Glycosylproteins.

Noel, Maxence; Gilormini, Pierre-André; Cogez, Virginie; Yamakawa, Nao; Vicogne, Dorothée; Lion, Cédric; Biot, Christophe; Guérardel, Yann; Harduin-Lepers, Anne.

Affiliation

Noel M; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Gilormini PA; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Cogez V; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Yamakawa N; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Vicogne D; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Lion C; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Biot C; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Guérardel Y; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.
Harduin-Lepers A; Université de Lille, CNRS, UMR 8576, UGSF, Unité de Glycobiologie Structurale et Fonctionnelle, 59000, Lille, France.

Chembiochem ; 18(13): 1251-1259, 2017 07 04.

Article in En | MEDLINE | ID: mdl-28395125

Subject(s)

Antigens, CD/metabolism; Cytidine Monophosphate N-Acetylneuraminic Acid/metabolism; Cytidine Monophosphate/analogs & derivatives; Glycolipids/metabolism; Glycoproteins/metabolism; Polysaccharides/metabolism; Sialic Acids/metabolism; Sialyltransferases/metabolism; Antigens, CD/chemistry; Antigens, CD/genetics; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Cloning, Molecular; Cytidine Monophosphate/chemistry; Cytidine Monophosphate/metabolism; Cytidine Monophosphate N-Acetylneuraminic Acid/chemistry; Gene Expression; Glycolipids/chemistry; Glycoproteins/chemistry; Glycoproteins/genetics; Glycosylation; HEK293 Cells; Humans; Kinetics; N-Acylneuraminate Cytidylyltransferase/genetics; N-Acylneuraminate Cytidylyltransferase/metabolism; Neisseria meningitidis/chemistry; Neisseria meningitidis/enzymology; Polysaccharides/chemistry; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sialic Acids/chemistry; Sialyltransferases/chemistry; Sialyltransferases/genetics; Substrate Specificity; beta-Galactoside alpha-2,3-Sialyltransferase

Key words

CMP-sialic acid; glycoengineering; selective exo enzymatic labeling; sialylation; sialyltransferases

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Polysaccharides / Sialic Acids / Sialyltransferases / Glycolipids / Glycoproteins / Antigens, CD / Cytidine Monophosphate / Cytidine Monophosphate N-Acetylneuraminic Acid Limits: Humans Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2017 Type: Article Affiliation country: France

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