Glycosylation—The Most Diverse Post-Translational Modification

Staudacher, Erika; Damme, Els J.M. Van; Smagghe, Guy

doi:10.3390/biom12091313

Cited by 3 publications

(2 citation statements)

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“…Studies have shown that phosphoserine residues can affect secondary protein structures and alter their biological activities and catalytic functions ( Shi, 2009 ). Site 107 of SOD3 is located close to the glycosylation modification site that may play an important role in the modification of translational and post-translational proteins ( Staudacher et al, 2022 ), suggesting that site 107 may alter the antioxidant activity of SOD3. Studies have shown that all SODs require a catalytic metal (Cu or Mn) for their activation ( Fukai and Ushio-Fukai, 2011 ; Skopp et al, 2019 ).…”

Section: Discussionmentioning

confidence: 99%

Adaptive evolution of antioxidase-related genes in hypoxia-tolerant mammals

Wang,

Luo,

et al. 2024

Front. Genet.

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To cope with the damage from oxidative stress caused by hypoxia, mammals have evolved a series of physiological and biochemical traits, including antioxidant ability. Although numerous research studies about the mechanisms of hypoxia evolution have been reported, the molecular mechanisms of antioxidase-related genes in mammals living in different environments are yet to be completely understood. In this study, we constructed a dataset comprising 7 antioxidase-related genes (CAT, SOD1, SOD2, SOD3, GPX1, GPX2, and GPX3) from 43 mammalian species to implement evolutionary analysis. The results showed that six genes (CAT, SOD1, SOD2, SOD3, GPX1, and GPX3) have undergone divergent evolution based on the free-ratio (M1) model. Furthermore, multi-ratio model analyses uncovered the divergent evolution between hypoxic and non-hypoxic lineages, as well as various hypoxic lineages. In addition, the branch-site model identified 9 positively selected branches in 6 genes (CAT, SOD1, SOD2, SOD3, GPX2, and GPX3) that contained 35 positively selected sites, among which 31 positively selected sites were identified in hypoxia-tolerant branches, accounting for 89% of the total number of positively selected sites. Interestingly, 65 parallel/convergent sites were identified in the 7 genes. In summary, antioxidase-related genes are subjected to different selective pressures among hypoxia-tolerant species living in different habitats. This study provides a valuable insight into the molecular evolution of antioxidase-related genes in hypoxia evolution in mammals.

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Section: Discussionmentioning

confidence: 99%

Adaptive evolution of antioxidase-related genes in hypoxia-tolerant mammals

Wang,

Luo,

et al. 2024

Front. Genet.

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“…Ribavirin) [10] (Figure 1a). N-glycosylation of the carboxamide side chain of glutamine (N-glycan) represents an important mode of posttranslational modification of proteins [11] . However, the distinct chemical properties of various nitrogen motifs, especially their basicity, also pose a significant challenge to the synthesis of N-glycosides [5] .…”

Section: Figure 1 Glycosyl Radical-mediated Synthesis Of N-glycosidesmentioning

confidence: 99%

Copper/photoredox catalysis enables desulfonylative radical N-glycosylation

Sun,

Wang,

Qin

et al. 2023

Preprint

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The state-of-the-art for glycosylation primarily relies on the classical polar reactions of heteroatomic nucleophiles with electrophilic glycosyl oxocarbenium intermediates. While such an ionic glycosylation strategy has worked well to deliver O-glycosides, its utilization in N-glycoside synthesis is often plagued by the subdued reactivity of N-nucleophiles under the acidic reaction conditions required for activating glycosyl donors. Exploring the reactivity of glycosyl radical intermediates could open up new glycosylation pathways. However, despite the recent significant progress in radical-mediated synthesis of C-glycosides, harnessing the reactivity of glycosyl radicals for the generation of canonical O- or N-glycosides remains elusive. Herein, we report the first examples of glycosyl radical-mediated N-glycosylation reaction using readily accessible glycosyl sulfone donors and N-nucleophiles under mild copper-catalyzed photoredox-promoted conditions. The method is efficient, selective, redox-neutral, and broadly applicable, enabling facile access to a variety of complex N-glycosides and nucleosides in a streamlined fashion. Importantly, the present system tolerates the presence of water and offers unique chemoselectivity, allowing selective reaction of NH sites over hydroxyl groups that would otherwise pose challenges in conventional cationic N-glycosylation.

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