PubMed:10369669 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":162},"obj":"Sentence"},{"id":"T2","span":{"begin":163,"end":333},"obj":"Sentence"},{"id":"T3","span":{"begin":334,"end":448},"obj":"Sentence"},{"id":"T4","span":{"begin":449,"end":611},"obj":"Sentence"},{"id":"T5","span":{"begin":612,"end":771},"obj":"Sentence"},{"id":"T6","span":{"begin":772,"end":985},"obj":"Sentence"}],"text":"Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum.\nUDP is generated in the lumen of the endoplasmic reticulum (ER) as a product of the UDP-glucose-dependent glycoprotein reglucosylation in the calnexin/calreticulin cycle. We describe here the identification, purification and characterization of an ER enzyme that hydrolyzes UDP to UMP. This nucleoside diphosphatase is a ubiquitously expressed, soluble 45 kDa glycoprotein devoid of transmembrane domains and KDEL-related ER localization sequences. It requires divalent cations for activity and hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. By eliminating UDP, which is an inhibitory product of the UDP-Glc:glycoprotein glucosyltransferase, it is likely to promote reglucosylation reactions involved in glycoprotein folding and quality control in the ER."}

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