ArticleThe Biochemical journal2001
Identification of the catalytic nucleophile of the Family 31 alpha-glucosidase from Aspergillus niger via trapping of a 5-fluoroglycosyl-enzyme intermediate.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 32 citations in OpenAlex.
- Characterization of Glycoside Hydrolase Families 13 and 31 Reveals Expansion and Diversification of α-Amylase Genes in the PhlebotomineFrontiers in physiology · 2021Article
- Development of a strategy for the screening of α-glucosidase-producing microorganisms.Journal of microbiology (Seoul, Korea) · 2020Article
- Prospecting for microbial α-The Journal of biological chemistry · 2019Article
- Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity.The Journal of biological chemistry · 2017Article
- Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes.ACS central science · 2016Article
- Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control.Scientific reports · 2016Article
- Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31.The Journal of biological chemistry · 2012Article
- Bioinformatic and biochemical studies point to AAGR-1 as the ortholog of human acid alpha-glucosidase in Caenorhabditis elegans.Molecular and cellular biochemistry · 2010Article
- NET37, a nuclear envelope transmembrane protein with glycosidase homology, is involved in myoblast differentiation.The Journal of biological chemistry · 2009Article
- A novel alpha-glucosidase from the acidophilic archaeon Ferroplasma acidiphilum strain Y with high transglycosylation activity and an unusual catalytic nucleophile.The Biochemical journal · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mechanism-based reagent 5-fluoro-alpha-d-glucopyranosyl fluoride (5F alpha GlcF) was used to trap a glycosyl-enzyme intermediate and identify the catalytic nucleophile at the active site of Aspergillus niger alpha-glucosidase (Family 31). Incubation of the enzyme with 5F alpha GlcF, followed by peptic proteolysis and comparative liquid chromatography/MS mapping allowed the isolation of a labelled peptide. Fragmentation analysis of this peptide by tandem MS yielded the sequence WYDMSE, with the label located on the aspartic acid residue (D). Comparison with the known protein sequence identified the labelled amino acid as Asp-224 of the P2 subunit.
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