A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

Eric Paul Bennett; Helle Hassan; Michael A. Hollingsworth; Henrik Clausen

doi:10.1016/S0014-5793(99)01268-5

A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

Eric Paul Bennett, Helle Hassan, Michael A. Hollingsworth, Henrik Clausen^*

^*Corresponding author for this work

107 Citations (Scopus)

Abstract

A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation. Copyright (C) 1999 Federation of European Biochemical Societies.

Original language	English
Journal	FEBS Letters
Volume	460
Issue number	2
Pages (from-to)	226-230
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/S0014-5793(99)01268-5
Publication status	Published - 29 Oct 1999

Keywords

GalNAc-transferase
Glycosyltransferase
Mucin
O-Glycosylation

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10.1016/S0014-5793(99)01268-5

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A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. / Bennett, Eric Paul; Hassan, Helle; Hollingsworth, Michael A. et al.

In: FEBS Letters, Vol. 460, No. 2, 29.10.1999, p. 226-230.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation. Copyright (C) 1999 Federation of European Biochemical Societies.",

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AU - Hassan, Helle

AU - Hollingsworth, Michael A.

AU - Clausen, Henrik

PY - 1999/10/29

Y1 - 1999/10/29

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AB - A novel member of the human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation. Copyright (C) 1999 Federation of European Biochemical Societies.

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KW - Glycosyltransferase

KW - Mucin

KW - O-Glycosylation

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A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates

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Keywords

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