134-61-2Relevant articles and documents
N-acetyltransferases from three different organisms displaying distinct selectivity toward hexosamines and N-terminal amine of peptides
Zhang, Peiru,Liu, Pei,Xu, Yangyang,Liang, Yulu,Wang, Peng George,Cheng, Jiansong
, p. 72 - 75 (2018/11/30)
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.
One-pot enzymatic production of 2-acetamido-2-deoxy-D-galactose (GalNAc) from 2-acetamido-2-deoxy-D-glucose (GlcNAc)
Inoue, Kousuke,Nishimoto, Mamoru,Kitaoka, Motomitsu
experimental part, p. 2432 - 2436 (2011/12/15)
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.
COMPOSITIONS AND METHODS FOR TREATING HEPATITIS-C
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, (2008/06/13)
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.