ArticleJournal of the American Chemical Society2017
Aspartate Glycosylation Triggers Isomerization to Isoaspartate.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Aspartimide Modification in RiPP Natural Products.Biochemistry · 2026Review
- Cysimiditides: RiPPs with a Zn-Tetracysteine Motif and Aspartimidylation.Biochemistry · 2025Article
- Surface protein glycosylation conserved in the human pathogen Mycoplasma genitalium and retained in the synthetic organism JCVI-Syn3A.PloS one · 2025Article
- Deciphering the Properties and Functions of Glycoproteins Using Quantitative Proteomics.Journal of proteome research · 2023Review
- OGT Protein Interaction Network (OGT-PIN): A Curated Database of Experimentally Identified Interaction Proteins of OGT.International journal of molecular sciences · 2021Article
- Effect of gold nanoparticles on the structure and neuroprotective function of protein L-isoaspartyl methyltransferase (PIMT).Scientific reports · 2021Article
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- An Unusually Rapid Protein Backbone Modification Stabilizes the Essential Bacterial Enzyme MurA.Biochemistry · 2020Article
- The O-GlcNAc Modification on Kinases.ACS chemical biology · 2020Article
- Article
- Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.Current opinion in structural biology · 2019Review
- O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.Journal of the American Chemical Society · 2018Article
- Post-Translational Modifications of Protein Backbones: Unique Functions, Mechanisms, and Challenges.Biochemistry · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
O-Linked β-N-acetylglucosamine transferase (OGT) is an essential human enzyme that glycosylates numerous nuclear and cytoplasmic proteins on serine and threonine. It also cleaves Host cell factor 1 (HCF-1) by a mechanism in which the first step involves glycosylation on glutamate. Replacing glutamate with aspartate in an HCF-1 proteolytic repeat was shown to prevent peptide backbone cleavage, but whether aspartate glycosylation occurred was not examined. We report here that OGT glycosylates aspartate much faster than it glycosylates glutamate in an otherwise identical model peptide substrate; moreover, once formed, the glycosyl aspartate reacts further to form a succinimide intermediate that hydrolyzes to produce the corresponding isoaspartyl peptide. Aspartate-to-isoaspartate isomerization in proteins occurs in cells but was previously thought to be exclusively non-enzymatic. Our findings suggest it may also be enzyme-catalyzed. In addition to OGT, enzymes that may catalyze aspartate to isoaspartate isomerization include PARPs, enzymes known to ribosylate aspartate residues in the process of poly(ADP-ribosyl)ation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.