14752-56-8Relevant articles and documents
Quantitative Standards of 4-O-Acetyl- and 9-O-Acetyl-N-Acetylneuraminic Acid for the Analysis of Plasma and Serum
Badia, Concepcion,Cheeseman, Jack,Gardner, Richard A.,Kuhnle, Gunter,Osborn, Helen M. I.,Spencer, Daniel I. R.,Thomson, Rebecca I.
, (2022/01/20)
N-Acetylneuraminic acid (sialic acid, Neu5Ac) is one of a large, diverse family of nine-carbon monosaccharides that play roles in many biological functions such as immune response. Neu5Ac has previously been identified as a potential biomarker for the presence and pathogenesis of cardiovascular disease (CVD), diabetes and cancer. More recent research has highlighted acetylated sialic acid derivatives, specifically Neu5,9Ac2, as biomarkers for oral and breast cancers, but advances in analysis have been hampered due to a lack of commercially available quantitative standards. We report here the synthesis of 9-O- and 4-O-acetylated sialic acids (Neu5,9Ac2 and Neu4,5Ac2) with optimisation of previously reported synthetic routes. Neu5,9Ac2 was synthesised in 1 step in 68 % yield. Neu4,5Ac2 was synthesised in 4 steps in 39 % overall yield. Synthesis was followed by analysis of these standards via quantitative NMR (qNMR) spectroscopy. Their utilisation for the identification and quantification of specific acetylated sialic acid derivatives in biological samples is also demonstrated.
Efficient whole-cell biocatalytic synthesis of N-Acetyl-D-neuraminic acid
Xu, Ping,Qiu, Jian Hua,Zhang, Yi Nan,Chen, Jing,Wang, Peng George,Yan, Bing,Song, Jing,Xi, Ri Mo,Deng, Zi Xin,Ma, Cui Qing
, p. 1614 - 1618 (2008/02/11)
N-Acetyl-D-neuraminic acid (Neu5Ac) was efficiently synthesized from lactate and a mixture of N-acetyl-D-glucosamine (GlcNAc) and N-acetyl-D-mannosamine (ManNAc) by whole cells. The biotransformation utilized Escherichia coli cells (Neu5Ac aldolase), Pseudomonas stutzeri cells (lactate oxidase components), GlcNAc/ManNAc and lactate. By this process, 18.32 ± 0.56 g/liter Neu5Ac were obtained from 65.61 ± 2.70 g/liter lactate as an initial substrate input. Neu5Ac (98.4 ± 0.4% purity, 80.87 ± 0.79% recovery yield) was purified by anionic exchange chromatography. Our results demonstrate that the reported Neu5Ac biosynthetic process can compare favorably with natural product extraction or chemical synthesis processes.
Enzymatic synthesis of cytidine 5′-monophospho-N-acetylneuraminic acid
Hamamoto, Tomoki,Takeda, So,Noguchi, Toshitada
, p. 1944 - 1950 (2008/02/04)
We have established an efficient method for enzymatic production of cytidine 5′-monophospho-N-acetylneuraminic acid (CMP-NeuAc) from inexpensive materials, N-acetylglucosamine (GlcNAc) and cytidine 5′-monophosphate (CMP). The Haemophilus influenzae nanE gene encoding GlcNAc 6-phosphate (GlcNAc 6-P) 2-epimerase and the Campylobacter jejuni neuB1 gene encoding N-acetylneuraminic acid (NeuAc) synthetase, both of whose products are involved in NeuAc biosynthesis, were cloned and co-expressed in Escherichia coli cells. We examined the synthesis of NeuAc from GlcNAc via GlcNAc 6-P, N-acetylmannosamine (ManNAc) 6-P, and ManNAc by the use of E. coli cells producing GlcNAc 6-P 2-epimerase and NeuAc synthetase, in expectation of biological functions of E. coli such as the supply of phosphoenolpyruvate (PEP), which is an essential substrate for NeuAc synthetase, GlcNAc phospholylation by the PEP-dependent phosphotransferase system, and dephospholylation of ManNAc 6-P. Eleven mM NeuAc was synthesized from 50 mM GlcNAc by recombinant E. coli cells with the addition of glucose as an energy source. Next we attempted to synthesize CMP-NeuAc from GlcNAc and CMP using yeast cells, recombinant E. coli cells, and H. influenzae CMP-Neu-Ac synthetase, and succeeded in efficient production of CMP-NeuAc due to a sufficient supply of PEP and efficient conversion of CMP to cytidine 5′-triphosphate by yeast cells.
