cas 1811-31-0, N-Acetyl-D-galactosamine | Articles data

Articles about 1811-31-0Total 7 be found

N-acetyltransferases from three different organisms displaying distinct selectivity toward hexosamines and N-terminal amine of peptides
N-acetyltransferases are a family of enzymes that catalyze the transfer of the acetyl moiety (–COCH3) from acetyl coenzyme A (Acetyl-CoA) to a primary amine of acceptor substrates from small molecules such as aminoglycoside to macromolecules of various proteins. In this study, the substrate selectivity of three N-acetyltransferases falling into different phylogenetic groups was probed against a series of hexosamines and synthetic peptides. GlmA from Clostridium acetobutylicum and RmNag from Rhizomucor miehei, which have been defined as glucosamine N-acetyltransferases, were herein demonstrated to be also capable of acetylating the free amino group on the very first glycine residue of peptide in spite of varied catalytic efficiency. The human recombinant N-acetyltransferase of Naa10p, however, prefers primary amine groups in the peptides as opposed to glucosamine. The varied preference of GlmA, RmNag and Naa10p probably arose from the divergent evolution of these N-acetyltransferases. The expanded knowledge of acceptor specificity would as well facilitate the application of these N-acetyltransferases in the acetylation of hexosamines or peptides.
Zhang, Peiru,Liu, Pei,Xu, Yangyang,Liang, Yulu,Wang, Peng George,Cheng, Jiansong
p. 72 - 75
(2018/11/30)

Structure and antioxidant activity study of sulfated acetamido- polysaccharide from Radix Hedysari
A new sulfated acetamido-heteropolysaccharide, HPS4-2A, was obtained by aqueous extraction followed by precipitation with ethanol and fractionation with DEAE column chromatography from Radix Hedysari. It was composed of rhamnose, arabinose, glucose, galactose and 2-acetamido-2-deoxy-D-galactose in the molar ratio of 10.09%:25.90%:25.90%:25.0%:12.30%. Elemental analysis indicated that HPS4-2A was a sulfated polysaccharide containing small amount of sulfate groups (1.87%). Partial acid hydrolysis, GC, GC-MS, 1D and 2D NMR spectroscopy analysis of the HPS4-2A revealed a predominance of glucose, galactose and 2-acetamido-2-deoxy-D-galactose linked in a highly-branched structure. Themolecular weight of HPS4-2Awas determined by HPSEC and HPSEC-MALLS. AFMstudy indicated that HPS4-2A took a highly branched conformation, which in consistent with the result studied by SEC-MALLS. Structural features of HPS4-2A were also investigated by SEM and TEM. Antioxidant assays demonstrated that HPS4-2A possessed of strong DPPH and hydroxyl radicals scavenging activities, suggesting that HPS4-2A could potentially be used as natural antioxidant.
Dang, Zilong,Feng, Demei,Liu, Xiaohua,Yang, Tao,Guo, Long,Liang, Jin,Liang, Jiandi,Hu, Fangdi,Cui, Fang,Feng, Shilan
p. 20 - 32
(2013/10/22)

Structure elucidation of the O-antigen of Salmonella enterica O51 and its structural and genetic relation to the O-antigen of Escherichia coli O23
The O-polysaccharide (O-antigen) of Salmonella enterica O51 was isolated by mild acid degradation of the lipopolysaccharide and its structure was established using sugar analysis and NMR spectroscopy. The O-antigen of Escherichia coli O23, whose structure was elucidated earlier, possesses a similar structure and differs only in the presence of an additional lateral α-D-Glcp residue at position 6 of the GlcNAc residue in the main chain. Sequencing of the O-antigen gene clusters of S. enterica O51 and E. coli O23 revealed the same genes with a high-level similarity. By comparison with opened gene databases, all genes expected for the synthesis of the common structure of the two O-antigens were assigned functions. It is suggested that the gene clusters of both bacteria originated from a common ancestor, whereas the O-antigen modification in E. coli O23, which, most probably, is induced by prophage genes outside the gene cluster, could be introduced after the species divergence.
Perepelov,Liu, Bin,Guo, Dan,Senchenkova,Shahskov,Feng, Lu,Wang, Lei,Knirel
experimental part
p. 774 - 779
(2012/01/19)

One-pot enzymatic production of 2-acetamido-2-deoxy-D-galactose (GalNAc) from 2-acetamido-2-deoxy-D-glucose (GlcNAc)
2-Acetamido-2-deoxy-D-galactose (GalNAc) is a common monosaccharide found in biologically functional sugar chains, but its availability is often limited due to the lack of abundant natural sources. In order to produce GalNAc from abundantly available sugars, 2-acetamido-2-deoxy-D-glucose (GlcNAc) was converted to GalNAc by a one-pot reaction using three enzymes involved in the galacto-N-biose/lacto-N-biose I pathway of bifidobacteria. Starting the reaction with 600 mM GlcNAc, 170 mM GalNAc was produced at equilibrium in the presence of catalytic amounts of ATP and UDP-Glc under optimized conditions. GalNAc was separated from GlcNAc using water-eluting cation-exchange chromatography with a commonly available cation-exchange resin.
Inoue, Kousuke,Nishimoto, Mamoru,Kitaoka, Motomitsu
experimental part
p. 2432 - 2436
(2011/12/15)

COMPOSITIONS AND METHODS FOR TREATING HEPATITIS-C
New compositions and methods for treating patients suffering from hepatitis-C, AIDS, aberrant apoptosis which include N-acetyl-D-glucosaminyl(β-1-4)-N-Acetyl-muramyl-L-ananyl-D-isoglutamine (GMDP) of at least 98% purity and provided either alone, as an active ingredient of blastolysine, or in combination with an aminosugar such as N-acetyl-glucosamine(NAG). The high purity GMDP has a decreased amount immunogenic impurities and demonstrates cell protection as opposed to solely immunostimulatory effects, while a synergistic cell protective effect is exhibited when GMDP in combined with NAG. The new compositions modulate FasL mediated apoptosis while simultaneously stimulating TNF-α production and further selectively inhibiting TNF-α receptor p55 (TNFR1), providing a treatment for patients suffering from hepatitis-C, AIDS or aberrant apoptosis.
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(2008/06/13)

A MECHANISTIC CONSIDERATION OF THE HYDRAZINOLYSIS OF 3-O-SUBSTITUTED 2-ACETAMIDO-2-DEOXY-D-HEXOPYRANOSYL AND -D-HEXITOL RESIDUES IN THE ABSENCE AND PRESENCE OF HYDRAZINIUM SULFATE
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Inoue, Yasuo,Kitajima, Ken
p. 342 - 348
(2007/10/02)

Structural studies of the O-specific side-chain of the lipopolysaccharide from Escherichia coli O 55.
The structure of the O-specific side-chains of the lipopolysaccharide from Escherichia coli O 55 has been investigated, methylation analysis, specific degradations, and n.m.r. spectroscopy being the principal methods used. It is concluded that the O-specific side-chains are composed of pentasaccharide repeating-units having the following structure [where Col stands for colitose (3,6-dideoxy-L-xylo-hexose)].(See formula in text).
Lindberg,Lindh,Loenngren
p. 105 - 112
(2007/10/02)