59830-12-5

Upstream product

• 108-24-7 acetic anhydride 
• 6734-92-5 chitosan hexamer 
• 13088-77-2 N,N',N'',N'''-tetraacetylchitotetraose 
• 439-02-1 2-acetamido-3,4,6-tri-O-acetyl-2-deoxy-α-D-glucopyranosyl fluoride 
• 10294-12-9 2-deoxy-2-acetamido-3,4,6-tri-O-acetyl-D-glucopyranose 
• 389-48-0 2-Acetamido-2-deoxy-α-D-glucopyranosyl fluoride 
• 14200-67-0 N,N'-diacetylchitobiose 
• 1420870-87-6 C₁₆H₂₇FN₂O₁₀ 

Downstream Products

• 7512-17-6 N-Acetyl-D-glucosamine 

Relevant academic research and scientific papers

A glycosynthase derived from an inverting GH19 chitinase from the moss Bryum coronatum

BcChi-A, a GH19 chitinase from the moss Bryum coronatum, is an endo-acting enzyme that hydrolyses the glycosidic bonds of chitin, (GlcNAc)n [a β-1,4-linked polysaccharide of GlcNAc (N-acetylglucosamine) with a polymerization degree of n], through an inverting mechanism. When the wild-type enzyme was incubated with α-(GlcNAc)2-F [α-(GlcNAc) 2 fluoride] in the absence or presence of (GlcNAc)2, (GlcNAc)2 and hydrogen fluoride were found to be produced through the Hehre resynthesis-hydrolysis mechanism. To convert BcChi-A into a glycosynthase, we employed the strategy reported by Honda et al. [(2006) J. Biol. Chem. 281, 1426-1431; (2008) Glycobiology 18, 325-330] of mutating Ser102, which holds a nucleophilic water molecule, and Glu 70, which acts as a catalytic base, producing S102A, S102C, S102D, S102G, S102H, S102T, E70G and E70Q. In all of the mutated enzymes, except S102T, hydrolytic activity towards (GlcNAc)6 was not detected under the conditions we used. Among the inactive BcChi-A mutants, S102A, S102C, S102G and E70G were found to successfully synthesize (GlcNAc)4 as amajor product from α-(GlcNAc)2-F in the presence of (GlcNAc) 2. The S102A mutant showed the greatest glycosynthase activity owing to its enhanced F- releasing activity and its suppressed hydrolytic activity. This is the first report on a glycosynthase that employs amino sugar fluoride as a donor substrate. The Authors Journal compilation

Efficient chemoenzymatic synthesis of lipo-chitin oligosaccharides as plant growth promoters

Lipo-chitin oligosaccharides (Nod and Myc LCOs) are molecules involved in symbiotic phenomena in the plant kingdom. They play a major role in the process of atmospheric nitrogen fixation and mineral soil nutrients uptake both in legumes and in non-legumes, and are active at extremely low concentrations down to the nano- and even picomolar range. These compounds contain various substitutions along the oligosaccharide backbone of the molecule including an essential fatty acid on the non-reducing unit and are considered as environmentally-friendly fertilizers. Currently, chemical synthesis cannot produce precursors of Nod and Myc LCOs at a large scale and an in vitro chemoenzymatic pathway is presented here as a new and efficient method for preparing quantities of these high-value oligosaccharides. VC1280 (Vibrio cholerae) is a chitin deacetylase (CD) capable of regioselectively cleaving an acetate from the non-reducing penultimate N-acetyl-d-glucosaminyl (GlcNAc) unit of chitin oligosaccharides (COs). This provides a free amino group which can be further N-acylated with a fatty-acid chain to give analogues of LCOs. Alternatively, the non-reducing GlcNAc unit can be removed by β-N-acetylglucosaminidase treatment, followed by N-acylation to give natural LCOs. VC1280 CD was produced in the periplasm of E. coli. Under the conditions used, 120 mg of the pure enzyme was recovered from 1 L of culture medium. For the first time, in vitro production of a library of natural LCOs as well as their analogues has been carried out at a preparative scale from biosourced chitin oligosaccharides constituting an approach of major interest for sustainable agriculture.

Introduction of a tryptophan side chain into subsite +1 enhances transglycosylation activity of a GH-18 chitinase from Arabidopsis thaliana, AtChiC

A tryptophan side chain was introduced into subsite +1 of family GH-18 (class V) chitinases from Nicotiana tabacum and Arabidopsis thaliana (NtChiV and AtChiC, respectively) by the mutation of a glycine residue to tryptophan (G74W-NtChiV and G75W-AtChiC). The specific activity toward glycol chitin of the two mutant enzymes was 70-71% of that of the wild type. Using chitin oligosaccharides, (GlcNAc)n (n = 4, 5 and 6), as the substrates, we found the transglycosylation reaction to be significantly enhanced in G74W-NtChiV and G75W-AtChiC when compared with the corresponding wild-type enzymes. The introduced tryptophan side chain might protect the oxazolinium ion intermediate from attack by a nucleophilic water molecule. The enhancement of transglycosylation activity was much more distinct in G75W-AtChiC than in G74W-NtChiV. Nuclear magnetic resonance titration experiments using the inactive double mutants, E115Q/G74W-NtChiV and E116Q/G75W-AtChiC revealed that the association constant of (GlcNAc)5 was considerably larger for the latter. Amino acid substitutions at the acceptor binding site might have resulted in the larger association constant for G75W-AtChiC, giving rise to the higher transglycosylation activity of G75W-AtChiC. The Author 2012. Published by Oxford University Press. All rights reserved.

Fucosylation of chitooligosaccharides by human α1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure

FUT8, a eukaryotic α1,6-fucosyltransferase, catalyzes the transfer of a fucosyl residue from guanine nucleotide diphosphate-β-L-fucose to the innermost GlcNAc of an asparagine-linked oligosaccharide (N-glycan). The catalytic domain of FUT8 is structurally

Synthesis of chitotetraose and chitohexaose based on dimethylmaleoyl protection

tert-Butyldimethylsilyl 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D-glucopyranoside was readily transformed into the disaccharide glycosyl donor, 3,4,6-tri-O-acetyl-2-deoxy-2-dimethylmaleimido-β-D-glucopyranosyl- (1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-α/β-D- glucopyranosyl trichloroacetimidate, and the disaccharide glycosyl acceptor, tert-butyldimethylsilyl 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D-glucopyranosyl- (1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D- glucopyranoside. A TMSOTf-catalysed coupling of the acceptor with the donor afforded the respective tetrasaccharide derivative, which can be transformed to chitotetraose. tert-Butyldimethylsilyl 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-4-O-phenoxyacetyl-β-D- glucopyranosyl-(1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido- β-D-glucopyranoside was converted into donor 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-4-O-phenoxyacetyl-β-D- glucopyranosyl-(1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido- β-D-glucopyranosyl trichloroacetimidate. Its coupling with benzyl 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D-glucopyranosyl- (1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D- glucopyranoside, followed by dephenoxyacetylation, gave benzyl 3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D-glucopyranosyl- (1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido-β-D- glucopyranosyl-(1→4)-3,6-di-O-benzyl-2-deoxy-2-dimethylmaleimido- β-D-glucopyranosyl-(1→4)-3,6-di-O-benzyl-2-deoxy-2- dimethylmaleimido-β-D-glucopyranoside, whose glycosylation furnished, after replacement of the DMM-group by the acetyl moiety and subsequent deprotection, chitohexaose.

Properties and Transglycosylation Reaction of a Chitinase from Nocardia orientalis

The hydrolytic products of a chitinase purified from Nocardia orientalis were examined on reduced (GlcNAc)n (n=2-6).The rate of hydrolysis on reduced (GlcNAc)4-6 increased with increasing chain-length of N-acetylglucosamine residues,