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A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5
(2006-12-13)
The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal ...
A specific short dextrin-hydrolyzing extracellular glucosidase from the thermophilic fungus Thermoascus aurantiacus 179-5
(2006-12-13)
The thermophilic fungus Thermoascus aurantiacus 179-5 produced large quantities of a glucosidase which preferentially hydrolyzed maltose over starch. Enzyme production was high in submerged fermentation, with a maximal ...
N-glycan trimming by glucosidase II is essential for Arabidopsis development
(Springer, 2008-10)
Glucosidase II, one of the early N-glycan processing enzymes and a major player in the glycoprotein folding quality control, has been described as a soluble heterodimer composed of alpha and beta subunits. Here we present ...
Glucosidase II beta subunit modulates N-glycan trimming in fission yeasts and mammals
(American Society for Cell Biology, 2009-07)
Glucosidase II (GII) plays a key role in glycoprotein biogenesis in the endoplasmic reticulum (ER). It is responsible for the sequential removal of the two innermost glucose residues from the glycan (Glc(3)Man(9)GlcNAc(2)) ...
Structure of the lectin mannose 6-phosphate receptor homology (MRH) domain of glucosidase II an enzyme that regulates glycoprotein folding quality control in the endoplasmic reticulum
(American Society for Biochemistry and Molecular Biology, 2013-06)
Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein ...
Structure of the Lectin MRH Domain of Glucosidase II, an Enzyme that Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum
(American Society For Biochemistry And Molecular Biology, 2013-04-05)
Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein ...
Glucosidase II and MRH-Domain Containing Proteins in the Secretory Pathway
(Bentham Science Publishers, 2015-01)
N-glycosylation in the endoplasmic reticulum (ER) consists of the transfer of a preassembled glycan conserved among species (Glc3Man9GlcNAc2) from a lipid donor to a consensus sequence within a nascent protein that is ...
Glucosidase II and N-glycan mannose content regulate the half-lives of monoglucosylated species in vivo
(American Society for Cell Biology, 2011-06)
Glucosidase II (GII) sequentially removes the two innermost glucose residues from the glycan (Glc3Man9GlcNAc2) transferred to proteins. GII also participates in cycles involving the lectin/chaperones calnexin (CNX) and ...
Crystal Structure and Functional Analyses of the Lectin Domain of Glucosidase II: Insights into Oligomannose Recognition
(American Chemical Society, 2015-07)
N-Glycans are modified as part of a quality control mechanism during glycoprotein folding in the endoplasmic reticulum (ER). Glucosidase II (GII) plays a critical role by generating monoglucosylated glycans that are ...