Ontology highlight
ABSTRACT:
SUBMITTER: Satoh T
PROVIDER: S-EPMC5079260 | biostudies-literature | 2016 Nov
REPOSITORIES: biostudies-literature
Satoh Tadashi T Toshimori Takayasu T Noda Masanori M Uchiyama Susumu S Kato Koichi K
Protein science : a publication of the Protein Society 20160914 11
The glycoside hydrolase family 31 (GH31) α-glucosidases play vital roles in catabolic and regulated degradation, including the α-subunit of glucosidase II (GIIα), which catalyzes trimming of the terminal glucose residues of N-glycan in glycoprotein processing coupled with quality control in the endoplasmic reticulum (ER). Among the known GH31 enzymes, only GIIα functions with its binding partner, regulatory β-subunit (GIIβ), which harbors a lectin domain for substrate recognition. Although the s ...[more]