Folding of Synthetic Homogeneous Glycoproteins in the Presence of a Glycoprotein Folding Sensor Enzyme

Autor:	Akira Seko, Akiko Kanamori, Masayuki Izumi, Simone Dedola, Yutaka Makimura, Masafumi Sakono, Yukishige Ito, Yasuhiro Kajihara
Rok vydání:	2014
Předmět:	chemistry.chemical_classification Protein Folding Spectrometry Mass Electrospray Ionization biology Chemistry Endoplasmic reticulum UGGT General Chemistry General Medicine Endoplasmic Reticulum Catalysis Substrate Specificity Folding (chemistry) Molecular recognition Enzyme Biochemistry Glucosyltransferases biology.protein Humans Glucosyltransferase Protein folding Glycoprotein Plant Proteins
Zdroj:	Angewandte Chemie. 126:2927-2931
ISSN:	0044-8249
DOI:	10.1002/ange.201309665
Popis:	UDP-glucose:glycoprotein glucosyltransferase (UGGT) plays a key role in recognizing folded and misfolded glycoproteins in the glycoprotein quality control system of the endoplasmic reticulum. UGGT detects misfolded glycoproteins and re-glucosylates them as a tag for misfolded glycoproteins. A flexible model to reproduce in vitro folding of a glycoprotein in the presence of UGGT in a mixture containing correctly folded, folding intermediates, and misfolded glycoproteins is described. The data demonstrates that UGGT can re-glucosylate all intermediates in the in vitro folding experiments, thus indicating that UGGT inspects not only final folded products, but also the glycoprotein folding intermediates.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::015938ee92b0ae983afc05872c468537 https://doi.org/10.1002/ange.201309665 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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