Introduction of a human- and keyboard-friendly N-glycan nomenclature

• Friedrich Altmann,
• Johannes Helm,
• Martin Pabst and
• Johannes Stadlmann

Beilstein J. Org. Chem. 2024, 20, 607–620, doi:10.3762/bjoc.20.53

• Toronto University taught us the term GnGn for the acceptor substrate of fucosyl transferases [28][29]. This “reductio ad essentialia” proved very helpful in our work with glycosyltransferases, e.g., insect hexosaminidase [30] and plant fucosyltransferase [31], which dealt with terminal modifications of

Synthesis, α-mannosidase inhibition studies and molecular modeling of 1,4-imino-ᴅ-lyxitols and their C-5-altered N-arylalkyl derivatives

• Martin Kalník,
• Sergej Šesták,
• Juraj Kóňa,
• Maroš Bella and
• Monika Poláková

Beilstein J. Org. Chem. 2023, 19, 282–293, doi:10.3762/bjoc.19.24

• compounds have been attracting attention due to their broad spectrum of biological activities [6]. A number of synthetic and naturally occurring iminosugars are able to inhibit various enzymes of medicinal interest including glycosidases, glycosyltransferases and many other carbohydrate processing enzymes

Cytochrome P450 monooxygenase-mediated tailoring of triterpenoids and steroids in plants

• Karan Malhotra and
• Jakob Franke

Beilstein J. Org. Chem. 2022, 18, 1289–1310, doi:10.3762/bjoc.18.135

• capacity to catalyse highly regio- and stereospecific reactions on complex substrates. Besides simple hydroxylations, they can also introduce oxo, carboxy, or epoxy moieties or double bonds. Such decorations often also enable additional layers of diversification by glycosyltransferases or acyltransferases

GlycoBioinformatics

• Kiyoko F. Aoki-Kinoshita,
• Frédérique Lisacek,
• Niclas Karlsson,
• Daniel Kolarich and
• Nicolle H. Packer

Beilstein J. Org. Chem. 2021, 17, 2726–2728, doi:10.3762/bjoc.17.184

• tightly connected to mainstream bioinformatics. For example, databases and tools from genomics can be used for gaining information about genes encoding for glycosyltransferases, glycosidases, and glycan-binding proteins (lectins), and search engines initially designed for the detection of

Progress and challenges in the synthesis of sequence controlled polysaccharides

• Giulio Fittolani,
• Theodore Tyrikos-Ergas,
• Denisa Vargová,
• Manishkumar A. Chaube and
• Martina Delbianco

Beilstein J. Org. Chem. 2021, 17, 1981–2025, doi:10.3762/bjoc.17.129

• (LG, e.g., phosphate, fluoride, nucleotide) are polymerized by the enzyme to form the desired polysaccharide (Figure 1A). Several classes of enzymes are available, including hydrolases, phosphorylases, sucrases, glycosyltransferases, and glycosynthases [19][20][21][22]. An excellent overview of the

A systems-based framework to computationally describe putative transcription factors and signaling pathways regulating glycan biosynthesis

• Theodore Groth,
• Rudiyanto Gunawan and
• Sriram Neelamegham

Beilstein J. Org. Chem. 2021, 17, 1712–1724, doi:10.3762/bjoc.17.119

• termed glycogenes [1][2]. These glycogenes include the glycosyltransferases, glycosidases, sulfotransferases, transporters, etc. The expression of these glycogenes is in turn driven by the action of a class of proteins called transcription factors (TFs). These TFs regulate gene expression by binding

Simulating the enzymes of ganglioside biosynthesis with Glycologue

• Andrew G. McDonald and
• Gavin P. Davey

Beilstein J. Org. Chem. 2021, 17, 739–748, doi:10.3762/bjoc.17.64

• ganglioside biosynthesis, and altered ganglioside status in cancer, and the effects on network structure are predicted. The simulator is available at the Glycologue website, https://glycologue.org/. Keywords: gangliosides; Glycologue; glycosyltransferases; neuropathy; Svennerholm nomenclature; Introduction

• negative charge. Figure 1 shows the structure of the monosialylated ganglioside GM1a. The biosynthesis of gangliosides occurs in the endoplasmic reticulum and Golgi, where specific glycosyltransferases act, in stepwise fashion, by adding monosaccharides from sugar nucleotide donors, first to ceramide, and

• longer accepted name and a reaction pattern. The reactions in Table 2 are based on activities of enzymes already classified within the IUBMB Enzyme List, or from the cited references, wherever an EC number is not available. Glycosyltransferases can act on a variety of substrates, and in cases where

Synthesis of C-glycosyl phosphonate derivatives of 4-amino-4-deoxy-α-ʟ-arabinose

• Lukáš Kerner and
• Paul Kosma

Beilstein J. Org. Chem. 2020, 16, 9–14, doi:10.3762/bjoc.16.2

• ; lipopolysaccharide; Introduction Glycosyltransferases are important enzymes that accomplish the transfer of activated sugar phosphates onto their respective acceptor molecules [1]. In most cases, nucleotide diphosphate sugars serve as the reactive species, but lipid-linked diphosphate derivatives are equally

• important, e.g., when connected to dolichol in mammalian systems or to undecaprenol in prokaryotic donor substrates for bacterial glycosyltransferases [2]. 4-Amino-4-deoxy-ʟ-arabinose (Ara4N) is an important microbial carbohydrate in bacterial lipopolysaccharides (LPS) and has been implicated in resistance

Lectins of Mycobacterium tuberculosis – rarely studied proteins

• Katharina Kolbe,
• Sri Kumar Veleti,
• Norbert Reiling and
• Thisbe K. Lindhorst

Beilstein J. Org. Chem. 2019, 15, 1–15, doi:10.3762/bjoc.15.1

• have been found in glycosyltransferases as well as in bacterial hydrolases [95]. The Mtb gene product of Rv1419 shows 41% amino acid sequence similarity to R-type lectins and encodes the Mtb protein sMTL-13 (see Figure 5 for secondary structure prediction and alignment with the ricin B-like lectin from

Semi-synthesis and insecticidal activity of spinetoram J and its D-forosamine replacement analogues

• Kai Zhang,
• Jiarong Li,
• Honglin Liu,
• Haiyou Wang and
• Lamusi A

Beilstein J. Org. Chem. 2018, 14, 2321–2330, doi:10.3762/bjoc.14.207

• of spinosyns via chemical modification [18]. Bioactivities of many microbial secondary metabolites are highly dependent on their sugar constituents which are transferred as nucleotide-activated sugars to an aglycon by glycosyltransferases [19]. Therefore, bioactivities of these metabolites could

Enzymatic synthesis of glycosides: from natural O- and N-glycosides to rare C- and S-glycosides

• Jihen Ati,
• Pierre Lafite and
• Richard Daniellou

Beilstein J. Org. Chem. 2017, 13, 1857–1865, doi:10.3762/bjoc.13.180

• Jihen Ati Pierre Lafite Richard Daniellou ICOA UMR CNRS 7311, University of Orléans, rue de Chartres, BP 6759, 45067 Orléans cedex 2, France 10.3762/bjoc.13.180 Abstract Carbohydrate related enzymes, like glycosyltransferases and glycoside hydrolases, are nowadays more easily accessible and are

• . Glycoside hydrolases (GHs) or glycosyltransferases (GTs) have been focused on in the search for glycosylation tools, and have been extensively studied for genetic engineering [9][10]. The corresponding compounds have proven useful in many applications ranging from glycosylation of natural products to

• current enzymatic methods described for the synthesis of unusual C- and S-glycosidic linkages, their mechanisms and the corresponding perspectives. Review Glycosyltransferases Glycosyltransferases (GTs, E.C. 2.4.1.x) catalyse the addition of a glycosyl moiety to an acceptor, using an activated sugar as

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

• circumventing the requirement to protect the other nucleophiles on the donor molecule. 2 Classical glycosylation strategies 2.1 Enzymatic strategies Chemoenzymatic glycosylation largely involves two classes of enzymes: glycosynthases engineered for the synthesis of oligosaccharides and glycosyltransferases for

• the complete absence of protecting groups in an aqueous environment using 2-chloro-1,3-dimethylimidazolinium chloride (DMC) and a mild amine base (NEt3) (see chapter 4.1). 2.1.2 Glycosyltransferases: Glycosyltransferases (GTs) catalyze the transfer of a carbohydrate from an activated nucleotide

• ]. On the other hand, the disadvantage is the need to synthesize NDP-sugars as substrates for the GT which is typically a multistep laborious process. Another particularly interesting application of glycosyltransferases is the chemoenzymatic synthesis of nucleosides. This is an incredibly powerful tool

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

• and solving the X-ray structure of this intermediate [75]. The A and B antigenic determinants are synthesised by the blood group A (GTA) and the blood group B (GTB) glycosyltransferases which transfer GalNAc from UDP-GalNAc for the A type and a Gal residue from UDP-Gal for the B-type. A mutant of the

Towards inhibitors of glycosyltransferases: A novel approach to the synthesis of 3-acetamido-3-deoxy-D-psicofuranose derivatives

• Maroš Bella,
• Miroslav Koóš and
• Chun-Hung Lin

Beilstein J. Org. Chem. 2015, 11, 1547–1552, doi:10.3762/bjoc.11.170

• computational methods. After the attempted thioglycosylation of 11 with EtSH in the presence of BF3·OEt2, 2-methyloxazoline derivatives 13 and 14 were isolated. Keywords: glycosyltransferases; inhibitors; D-psicofuranose; synthesis; thioglycosylation; Introduction Glycosyltransferases (GTs) belong to a family

• ][4]. In addition, the role played by the glycoconjugates changes markedly during disease development such as malignant transformation [5], cancer cell proliferation and metastases spreading [6]. Since glycosyltransferases (GTs) are entailed in the biosynthesis of glycans and glycoconjugates, which

• are involved in these disease processes, inhibitors of GTs are of great therapeutic potential and attract remarkable interest for drug development. Although the mechanism of reactions catalyzed by glycosyltransferases has been investigated thoroughly, many aspects of the catalytic mechanism remain

Synthesis of a hexasaccharide partial sequence of hyaluronan for click chemistry and more

• Marina Bantzi,
• Stephan Rigol and
• Athanassios Giannis

Beilstein J. Org. Chem. 2015, 11, 604–607, doi:10.3762/bjoc.11.67

• not form PGs, in contrast to the other GAGs, which are synthesized in the Golgi apparatus or the endoplasmic reticulum [8]. HA is enzymatically produced by three glycosyltransferases (HA synthases: HAS 1, 2 and 3) in the cellular plasma membrane and its chain can reach a mass of 102–104 kDa [9

Studies on the substrate specificity of a GDP-mannose pyrophosphorylase from Salmonella enterica

• Lu Zou,
• Ruixiang Blake Zheng and
• Todd L. Lowary

Beilstein J. Org. Chem. 2012, 8, 1219–1226, doi:10.3762/bjoc.8.136

• synthesis; kinetics; methylation; pyrophosphorylase; sugar nucleotide; Introduction Modified sugar nucleotide analogues are valuable probes to study glycosyltransferases and other enzymes that use these activated glycosylating agents as substrates [1][2][3][4][5]. The synthesis of natural and non-natural

The use of glycoinformatics in glycochemistry

• Thomas Lütteke

Beilstein J. Org. Chem. 2012, 8, 915–929, doi:10.3762/bjoc.8.104

• their biosynthesis: DNA, RNA and proteins are synthesized by copying, transcription or translation, respectively, of nucleic acids, whereas carbohydrates are built in a non-template-driven approach by the sequential action of various glycosyltransferases (GT) that add monosaccharides to an existing

• major chemical databases would not only make it easier to find specific carbohydrates, but also provide a linkage between biological and chemical information. Databases on glycosyltransferases and glycan binding proteins As an alternative or complement to chemical synthesis it is possible to make use of

• the enzymes that build or degrade the glycan chains in vivo, the glycosyltransferases or glycoside hydrolases, respectively [46][47][48][49]. To plan such experiments, however, detailed knowledge of the substrate-specificity of these enzymes is required. The same applies to glycan-binding proteins

Synthetic glycopeptides and glycoproteins with applications in biological research

• Ulrika Westerlind

Beilstein J. Org. Chem. 2012, 8, 804–818, doi:10.3762/bjoc.8.90

• water-soluble radical initiator VA-044 [73]. The radical-induced desulfurization method has also been applied in the total synthesis of an EPO glycoprotein analogue [69]. Another promising path to prepare homogenous glycoproteins is represented by chemoenzymatic synthesis. Both glycosyltransferases and

• glycopeptide/glycoprotein synthesis, Endo-A specific for high-mannose glycans and Endo-M operating on both high-mannose and complex type N-glycans [81][82][83]. These enzymes can, in contrast to glycosyltransferases, by means of a one-step reaction attach large oligosaccharides to a GlcNAc polypeptide. Until

Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

• Christiane E. Kupper,
• Ruben R. Rosencrantz,
• Birgit Henßen,
• Helena Pelantová,
• Stephan Thönes,
• Anna Drozdová,
• Vladimir Křen and
• Lothar Elling

Beilstein J. Org. Chem. 2012, 8, 712–725, doi:10.3762/bjoc.8.80

• quantitative yield. In this way defined oxidised poly-LacNAc oligomer structures are easily obtained by galactose oxidase treatment and subsequent heating of the reaction mixture. The corresponding 6-aldehyde LacNAc oligomers were used as substrates in further elongation reactions with glycosyltransferases

• poly-LacNAc glycans 15a,b (see Scheme 3B) were tested as substrates for further enzymatic conversion with β3GlcNAc-transferase and MBP-His6-α3Gal-transferase [45][54] on an analytical scale. HPLC analysis indicated that 3a,b as well as 15a,b were accepted as substrates by both glycosyltransferases

• (Figure 2 and Figure S8 in Supporting Information File 1). In contrast, the α,β-unsaturated aldehydes 7a,b are not accepted as substrates by the tested glycosyltransferases. The reaction of 3a with β3GlcNAc-transferase (Scheme 2A) was analysed by ESI–MS (Table S1 and Figure S13 in Supporting Information

Sonogashira–Hagihara reactions of halogenated glycals

• Dennis C. Koester and
• Daniel B. Werz

Beilstein J. Org. Chem. 2012, 8, 675–682, doi:10.3762/bjoc.8.75

• ][3][4]. Many different monosaccharide units and the large variety of possibilities to link two subunits result in an immense variety of highly complex biomolecules [5][6][7]. In order to mimic certain subunits of oligosaccharides, e.g., for the inhibition of glycosidases or glycosyltransferases

Methods for the synthesis of polyhydroxylated piperidines by diastereoselective dihydroxylation: Exploitation in the two-directional synthesis of aza-C-linked disaccharide derivatives

• Andrew Kennedy,
• Adam Nelson and
• Alexis Perry

Beilstein J. Org. Chem. 2005, 1, No. 2, doi:10.1186/1860-5397-1-2

• LS2 9JT, UK School of Chemistry, University of Leeds, Leeds LS2 9JT, UK 10.1186/1860-5397-1-2 Abstract Background Many polyhydroxylated piperidines are inhibitors of the oligosaccharide processing enzymes, glycosidases and glycosyltransferases. Aza-C-linked disaccharide mimetics are compounds in

• polyhydroxylated piperidines are potent inhibitors of the oligosaccharide processing enzymes, glycosidases and glycosyltransferases.[1][2][3] For example, deoxymannojirimycin, 1, and deoxynojirimycin, 2, are selective mannosidase and glucosidase inhibitors respectively.[4][5] In these molecules, the nitrogen atom