The effect of neighbouring group participation and possible long range remote group participation in O-glycosylation

• Rituparna Das and
• Balaram Mukhopadhyay

Beilstein J. Org. Chem. 2025, 21, 369–406, doi:10.3762/bjoc.21.27

• significantly spurred the scientific curiosity of researchers over the past few decades [1]. Intensive studies revealed that this subtle code of cell surface glycans is extensively responsible for monitoring a plethora of diverse biological phenomena like post-translational modification of proteins [2][3

Discovery of antimicrobial peptides clostrisin and cellulosin from Clostridium: insights into their structures, co-localized biosynthetic gene clusters, and antibiotic activity

• Moisés Alejandro Alejo Hernandez,
• Katia Pamela Villavicencio Sánchez,
• Rosendo Sánchez Morales,
• Karla Georgina Hernández-Magro Gil,
• David Silverio Moreno-Gutiérrez,
• Eddie Guillermo Sanchez-Rueda,
• Yanet Teresa-Cruz,
• Brian Choi,
• Armando Hernández Garcia,
• Alba Romero-Rodríguez,
• Oscar Juárez,
• Siseth Martínez-Caballero,
• Mario Figueroa and
• Corina-Diana Ceapă

Beilstein J. Org. Chem. 2024, 20, 1800–1816, doi:10.3762/bjoc.20.159

• is recognized by post-translational enzymes and a core peptide where these enzymes produce the formation of Dha-Cys or Dhb-Cys residues. The post-translational modification enzymes involved span different functional domains (a cyclase and a dehydratase), and their activity is tightly controlled at

• biochemical conditions that we have not yet identified. At this point, based on the information we have gathered, we have been unable to explain the lack of post-translational modification. Although we attempted experiments to mix the CloM2 enzyme with the CloA1 precursor peptide and to mix the CloM1 enzyme

• -translational modification enzymes The selected supercluster is predicted to be formed by two adjacent, biosynthetically complete transcriptional units, each with specific promoter and terminator sites (Figure 2) containing two LanM enzymes (CloM1 and CloM2), the precursor peptides CloA1 and CloA2, as well as

Methyltransferases from RiPP pathways: shaping the landscape of natural product chemistry

• Maria-Paula Schröder,
• Isabel P.-M. Pfeiffer and
• Silja Mordhorst

Beilstein J. Org. Chem. 2024, 20, 1652–1670, doi:10.3762/bjoc.20.147

• encoded in the same BGC as the precursor peptide install post-translational modifications in the core peptide. Finally, a protease releases the modified core peptide, creating the mature natural product [2]. The transfer of a methyl group is a common post-translational modification in RiPP biosynthesis

• producing divamide A. Divamide A contains a trimethylated glutamate at the N-terminus (Figure 4), which is installed by DivMT as the final step in divamide A biosynthesis. The presence of the cyclic lysinoalanine moiety is required for this post-translational modification. The addition of other N-terminal

¹⁹F NMR as a tool in chemical biology

• Diana Gimenez,
• Aoife Phelan,
• Cormac D. Murphy and
• Steven L. Cobb

Beilstein J. Org. Chem. 2021, 17, 293–318, doi:10.3762/bjoc.17.28

• are being investigated that enable the enzymatic post-translational modification of non-nucleophilic residues, such as glutamate [31]. As recently demonstrated by Kojima and co-workers, recombinant protein transglutaminase (TGase) could be used to catalyse the chemical replacement of the γ

GlypNirO: An automated workflow for quantitative N- and O-linked glycoproteomic data analysis

• Toan K. Phung,
• Cassandra L. Pegg and
• Benjamin L. Schulz

Beilstein J. Org. Chem. 2020, 16, 2127–2135, doi:10.3762/bjoc.16.180

• -glycosylation; O-glycosylation; Python; Introduction Glycosylation is a key post-translational modification critical for protein folding and function in eukaryotes [1][2][3]. Diverse types of glycosylation are known, all involving modification of specific amino acid residues with complex carbohydrate

Synthesis of new asparagine-based glycopeptides for future scanning tunneling microscopy investigations

• Laura Sršan and
• Thomas Ziegler

Beilstein J. Org. Chem. 2020, 16, 888–894, doi:10.3762/bjoc.16.80

• pathogenesis [1][2][3][4]. Glycosylation is also considered to be one of the most important post-translational modification (PTM) since more than half of all human proteins are glycopeptides or glycoproteins [5]. Therefore, understanding how glycopeptides interact on an intra- and intermolecular level is

Strategies toward protecting group-free glycosylation through selective activation of the anomeric center

• A. Michael Downey and
• Michal Hocek

Beilstein J. Org. Chem. 2017, 13, 1239–1279, doi:10.3762/bjoc.13.123

• ; Review 1 Introduction The glycosylation reaction is of extreme importance in nature as it is possibly the most prevalent post-translational modification and thus has implications in a tremendous number of biological processes, including diseases [1]. More expedient chemical and enzymatic methods to

Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience

• Serge Pérez and
• Daniele de Sanctis

Beilstein J. Org. Chem. 2017, 13, 1145–1167, doi:10.3762/bjoc.13.114

• glycosylated, whereas proteins expressed in E. coli do not contain any glycan chains. For proteins that require post-translational modification, eukaryotic expression systems are usually preferred [30]. The crystallization of glycoproteins faces several obstacles, including the micro-heterogenity of glycans at

Posttranslational isoprenylation of tryptophan in bacteria

• Masahiro Okada,
• Tomotoshi Sugita and
• Ikuro Abe

Beilstein J. Org. Chem. 2017, 13, 338–346, doi:10.3762/bjoc.13.37

• ; isoprenylation; post-translational modification; quorum sensing; tryptophan; Introduction Posttranslational modification is the chemical modification of proteins after their translation from mRNAs to the corresponding polypeptide chains synthesized by ribosomes. Since a posttranslational modification generates

• . Therefore, posttranslational modifications dynamically regulate the biological activities of proteins. Novel modifications have been discovered over the last several decades, revealing numerous post-translational modification patterns, including isoprenylation [1][2]. This review will discuss the

From supramolecular chemistry to the nucleosome: studies in biomolecular recognition

• Marcey L. Waters

Beilstein J. Org. Chem. 2016, 12, 1863–1869, doi:10.3762/bjoc.12.175

• -helices; aromatic interactions; β-hairpin peptides; cation–π interactions; dynamic combinatorial chemistry; histone; molecular recognition in water; nucleosome; π–π-stacking; post-translational modification; supramolecular chemistry; Review Childhood influences When thinking about how to start writing

• structure of a protein that binds to trimethyllysine (KMe3), an important post-translational modification involved in controlling gene expression, shows that it recognizes the trimethylammonium group via an aromatic cage (Figure 6a) [39]. This suggests that the binding is driven by cation–π interactions. We

Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides

• Andrew W. Truman

Beilstein J. Org. Chem. 2016, 12, 1250–1268, doi:10.3762/bjoc.12.120

• predictably than molecules made from multi-domain megasynthases such as polyketides and non-ribosomal peptides. Cyclisation is a common post-translational modification in RiPP pathways and includes a multitude of transformations. These modifications are usually essential for the proper biological activity of

Profluorescent substrates for the screening of olefin metathesis catalysts

• Raphael Reuter and
• Thomas R. Ward

Beilstein J. Org. Chem. 2015, 11, 1886–1892, doi:10.3762/bjoc.11.203

• recent applications, metathesis has also been used in chemical biology, either in the form of an artificial metalloenzyme [8][9][10] or for the post-translational modification of proteins [11]. To address these various challenges, a vast number of carbene complexes based on different transition metals

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• in microorganisms Microbial natural products of the peptide class are produced by two types of biosynthetic pathways: By giant multi-domain enzymes, the nonribosomal peptide synthetases (NRPS) or by ribosomal synthesis and subsequent post-translational modification and processing. NRPS consist of

• and a core peptide. Associated post-translational modification enzymes (PTMs) catalyze different types of macrocyclizations of the core peptide and side-chain modifications of amino acids. Peptide maturation further requires cleavage of the leader peptide by processing proteases (PP) frequently

• Microcystis and Planktothrix [64][65]. Post-translational modification of microviridins is achieved by the activity of two closely related ATP grasp ligases, MdnB and MdnC (MvdC and D in Planktothrix). The enzymes introduce two ω-ester linkages between threonine and aspartate and serine and glutamate (MdnC

Synthesis of glycosylated β³-homo-threonine conjugates for mucin-like glycopeptide antigen analogues

• Florian Karch and
• Anja Hoffmann-Röder

Beilstein J. Org. Chem. 2010, 6, No. 47, doi:10.3762/bjoc.6.47

• increased biological half-life. Keywords: glycopeptide; glycosylamino acids; β3-homo-threonine; MUC1 antigens; solid-phase synthesis; Introduction Glycosylation is the predominant co- and post-translational modification in higher organisms responsible for tailoring and fine-tuning of the activity of