Automated chemical oligosaccharide synthesis is an attractive concept that has been successfully applied to a large number of target structures, but requires excess quantities of suitably protected and activated building blocks. Herein we demonstrate the use of biocatalysis to supply such reagents for automated synthesis. By using the promiscuous NmLgtB-B β1-4 galactosyltransferase from Neisseria meningitidis we demonstrate fast and robust access to the LacNAc motif, common to many cell-surface glycans, starting from either lactose or sucrose as glycosyl donors. The enzymatic product was shown to be successfully incorporated as a complete unit into a tetrasaccharide target by automated assembly.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7756758PMC
http://dx.doi.org/10.1002/anie.202008067DOI Listing

Publication Analysis

Top Keywords

enzymatic building-block
4
building-block synthesis
4
synthesis solid-phase
4
automated
4
solid-phase automated
4
automated glycan
4
glycan assembly
4
assembly automated
4
automated chemical
4
chemical oligosaccharide
4

Similar Publications

Polycyclic tetramate macrolactams (PoTeMs) represent a growing class of bioactive natural products that are derived from a common tetramate polyene precursor, lysobacterene A, produced by an unusual bacterial iterative polyketide synthase (PKS) / non-ribosomal peptide synthetase (NRPS). The structural and functional diversity of PoTeMs is biosynthetically elaborated from lysobacterene A by pathway-specific cyclizing and modifying enzymes. This results in diverse core structure decoration and cyclization patterns.

View Article and Find Full Text PDF

Enzymatic Ring Contraction for the Biosynthesis of Sulfur-Containing Cyclopentachromone.

J Am Chem Soc

January 2025

Department of Chemical and Biomolecular Engineering, University of Pennsylvania, Philadelphia, Pennsylvania19104, United States.

Cyclopentachromone, distinguished by its 6/6/5 heterotricyclic ring structure, is a key building block in many bioactive natural products, yet its enzymatic origin remains unclear. We identified a new class of cyclopentachromone-containing compounds, termed isochromosulfines, characterized by unique C-S bonds. A distinct FAD-dependent monooxygenase, IscL, was identified to catalyze the formation of the 6/6/5 cyclopentadiene intermediate, 2-remisporine A, from a 6/6/6 xanthone precursor via benzene ring contraction.

View Article and Find Full Text PDF

Enzymatic Kinetic Resolution of Racemic 1-(Isopropylamine)-3-phenoxy-2-propanol: A Building Block for β-Blockers.

Int J Mol Sci

October 2024

Department of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, Poland.

This study aimed to optimize the kinetic resolution of building blocks for the synthesis of β-blockers using lipases, which could be potentially used to synthesize enantiomerically pure β-blockers further. Reaction mixtures were incubated in a thermostated shaker. Qualitative and quantitative analyses of the reaction mixtures were performed using chiral stationary phases and the UPLC-IT-TOF system.

View Article and Find Full Text PDF

Valorization of levulinic acid by esterification with 1-octanol using a novel biocatalyst derived from Araujia sericifera.

J Biotechnol

November 2024

Departamento de Ingeniería Química, Universidad Nacional del Sur (UNS), Avda. Alem 1253, Bahía Blanca 8000, Argentina; Planta Piloto de Ingeniería Química - PLAPIQUI (UNS - CONICET), Camino La Carrindanga Km 7, CC 717, Bahía Blanca 8000, Argentina. Electronic address:

Levulinic acid, which can be obtained from biomass, has sparked great interest as a biologically-based chemical building block with wide versatility and potential. Its esterification with alcohols of different chain lengths is a promising valorization process for obtaining esters with various applications in the areas of biofuels/biolubricants, food and cosmetics, among others. In this work, the enzymatic esterification of levulinic acid and 1-octanol using a biocatalyst derived from Araujia sericifera latex was studied in systems with and without solvent.

View Article and Find Full Text PDF

Isonitrile biosynthesis by non-heme iron(II)-dependent oxidases/decarboxylases.

Methods Enzymol

September 2024

Department of Chemical and Biomolecular Engineering, University of California, Berkeley, CA, United States. Electronic address:

The isonitrile group is a compact, electron-rich moiety coveted for its commonplace as a building block and bioorthogonal functionality in synthetic chemistry and chemical biology. Hundreds of natural products containing an isonitrile group with intriguing bioactive properties have been isolated from diverse organisms. Our recent discovery of a conserved biosynthetic gene cluster in some Actinobacteria species highlighted a novel enzymatic pathway to isonitrile formation involving a non-heme iron(II) and α-ketoglutarate-dependent dioxygenase.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!