scholarly journals Unusual Transglycosylation Activity of Flavobacterium meningosepticum Endoglycosidases Enables Convergent Chemoenzymatic Synthesis of Core Fucosylated Complex N-Glycopeptides

ChemBioChem ◽  
2011 ◽  
Vol 12 (6) ◽  
pp. 932-941 ◽  
Author(s):  
Wei Huang ◽  
Jie Li ◽  
Lai-Xi Wang
Keyword(s):  
Chemoenzymatic Synthesis ◽  
Transglycosylation Activity ◽  
Flavobacterium Meningosepticum

A One-Pot Chemoenzymatic Synthesis of (2S,4R)-4-Methylproline Enables the First Total Synthesis of Antiviral Lipopeptide Cavinafungin B

2018 ◽  
Author(s):  
Christian R. Zwick ◽  
Hans Renata
Keyword(s):  
Total Synthesis ◽  
Natural Product ◽  
Complex Molecule ◽  
Molecular Target ◽  
Chemoenzymatic Synthesis ◽  
General Strategy ◽  
One Pot

We report an efficient ten-step synthesis of antiviral natural product cavinafungin B in 37% overall yield. By leveraging a one-pot chemoenzymatic synthesis of (2S,4R)-4-methylproline and oxazolidine-tethered (Rink-Boc-ATG-resin) SPPS methodology, the assembly of our molecular target could be conducted in an efficient manner.This general strategy could prove amenable to the construction of other natural and unnatural linear lipopeptides. The value of incorporating biocatalytic steps in complex molecule synthesis is highlighted by this work.

Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application

Biologia ◽  
2009 ◽  
Vol 64 (6) ◽  
Author(s):  
Yue-Hong Wang ◽  
Yu Jiang ◽  
Zuo-Ying Duan ◽  
Wei-Lan Shao ◽  
Hua-Zhong Li
Keyword(s):  
Escherichia Coli ◽  
Heat Shock ◽  
Optimal Condition ◽  
Industrial Application ◽  
Conversion Rate ◽  
Hydrolytic Activity ◽  
Thermoanaerobacter Ethanolicus ◽  
Transglycosylation Activity

AbstractIn this study, a new α-glucosidase gene from Thermoanaerobacter ethanolicus JW200 was cloned and expressed in Escherichia coli by a novel heat-shock vector pHsh. The recombinant α-glucosidase exhibited its maximum hydrolytic activity at 70°C and pH 5.0∼5.5. With p-nitrophenyl-α-D-glucoside as a substrate and under the optimal condition (70°C, pH 5.5), K m and V max of the enzyme was 1.72 mM and 39 U/mg, respectively. The purified α-glucosidase could hydrolyze oligosaccharides with both α-1,4 and α-1,6 linkages. The enzyme also had strong transglycosylation activity when maltose was used as sugar donor. The transglucosylation products towards maltose are isomaltose, maltotriose, panose, isomaltotriose and tetrasaccharides. The enzyme could convert 400 g/L maltose to oligosaccharides with a conversion rate of 52%, and 83% of the oligosaccharides formed were prebiotic isomaltooligosaccharides (containing isomaltose, panose and isomaltotriose).

scholarly journals Molecular cloning and amino acid sequence of peptide-N4-(N-acetyl-beta-D-glucosaminyl)asparagine amidase from flavobacterium meningosepticum.

1990 ◽  
Vol 265 (12) ◽  
pp. 6961-6966
Author(s):  
A L Tarentino ◽  
G Quinones ◽  
A Trumble ◽  
L M Changchien ◽  
B Duceman ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Cloning ◽  
Flavobacterium Meningosepticum

scholarly journals Recent Advances in the Chemical Biology of N-Glycans

Molecules ◽  
2021 ◽  
Vol 26 (4) ◽  
pp. 1040
Author(s):  
Asuka Shirakawa ◽  
Yoshiyuki Manabe ◽  
Koichi Fukase
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Molecular Basis ◽  
Chemical Biology ◽  
Molecular Level ◽  
Chemoenzymatic Synthesis ◽  
Complex Structures ◽  
Recent Advances ◽  
Protein Functions ◽  
Potential Applications

Asparagine-linked N-glycans on proteins have diverse structures, and their functions vary according to their structures. In recent years, it has become possible to obtain high quantities of N-glycans via isolation and chemical/enzymatic/chemoenzymatic synthesis. This has allowed for progress in the elucidation of N-glycan functions at the molecular level. Interaction analyses with lectins by glycan arrays or nuclear magnetic resonance (NMR) using various N-glycans have revealed the molecular basis for the recognition of complex structures of N-glycans. Preparation of proteins modified with homogeneous N-glycans revealed the influence of N-glycan modifications on protein functions. Furthermore, N-glycans have potential applications in drug development. This review discusses recent advances in the chemical biology of N-glycans.

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