Structure and mechanism of the ER-based glucosyltransferase ALG6.
Biocatalysis
Catalytic Domain
Conserved Sequence
Cryoelectron Microscopy
Dolichol Monophosphate Mannose
/ metabolism
Dolichol Phosphates
/ metabolism
Endoplasmic Reticulum
/ enzymology
Glucose
/ analogs & derivatives
Glycosyltransferases
/ deficiency
In Vitro Techniques
Lipids
Membrane Proteins
/ deficiency
Models, Molecular
Mutation
Polyisoprenyl Phosphate Monosaccharides
/ chemistry
Protein Binding
Saccharomyces cerevisiae
/ enzymology
Saccharomyces cerevisiae Proteins
/ genetics
Substrate Specificity
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
26
08
2019
accepted:
06
01
2020
pubmed:
28
2
2020
medline:
14
4
2020
entrez:
28
2
2020
Statut:
ppublish
Résumé
In eukaryotic protein N-glycosylation, a series of glycosyltransferases catalyse the biosynthesis of a dolichylpyrophosphate-linked oligosaccharide before its transfer onto acceptor proteins
Identifiants
pubmed: 32103179
doi: 10.1038/s41586-020-2044-z
pii: 10.1038/s41586-020-2044-z
pmc: PMC8712213
mid: NIHMS1753963
doi:
Substances chimiques
Dolichol Phosphates
0
Lipids
0
Membrane Proteins
0
Polyisoprenyl Phosphate Monosaccharides
0
Saccharomyces cerevisiae Proteins
0
dolichol monophosphate
12698-55-4
Dolichol Monophosphate Mannose
55598-56-6
dolichol-D-glucosylmonophosphate
55607-88-0
Glycosyltransferases
EC 2.4.-
ALG6 protein, S cerevisiae
EC 2.4.1.267
Glucose
IY9XDZ35W2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
443-447Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM117372
Pays : United States
Organisme : NIH HHS
ID : GM117372
Pays : United States
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