98300-80-2

Usage

Uses

Used in Biomedical Research:
CMP-Neu5Gc is utilized as a research subject for understanding its role in chronic inflammation, cancer, and autoimmune diseases. Its incorporation into human tissues through dietary sources has been linked to these health issues, providing insights into the molecular mechanisms underlying these conditions.
Used in Nutritional Studies:
CMP-Neu5Gc is employed as a nutritional marker to investigate the impact of dietary sources, such as red meat and dairy products, on human health. Studying its presence in human cells can help develop dietary recommendations and interventions to mitigate the potential risks associated with its consumption.
Used in Drug Development:
CMP-Neu5Gc may be explored as a target for drug development, focusing on modulating its levels or activity in human cells. Developing therapeutic agents that can regulate CMP-Neu5Gc could potentially offer novel treatment options for chronic inflammation, cancer, and autoimmune diseases.
Used in Diagnostics:
CMP-Neu5Gc can be employed as a biomarker for the early detection and monitoring of diseases associated with its presence in human cells. Measuring its levels in biological samples may aid in the diagnosis and prognosis of chronic inflammation, cancer, and autoimmune diseases.

InChI:InChI=1/C20H31N4O17P/c21-10-1-2-24(19(35)22-10)17-15(32)14(31)9(39-17)6-38-42(36,37)41-20(18(33)34)3-7(27)12(23-11(29)5-26)16(40-20)13(30)8(28)4-25/h1-2,7-9,12-17,25-28,30-32H,3-6H2,(H,23,29)(H,33,34)(H,36,37)(H2,21,22,35)/t7-,8+,9+,12+,13+,14+,15+,16+,17?,20+/m0/s1

Upstream product

• 80124-69-2 5-glycolylamido-3,5-dideoxy-D-glycero-D-galacto-2-nonulopyranosylonic acid 
• 65-47-4 cytidine triphosphate 
• 113-24-6 sodium pyruvate 
• 175877-09-5 2',3'-O,N⁴-triacetylcytidin-5'-yl methyl 5-[2-(acetoxy)acetamido]-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-β-D-glycero-D-galacto-2-nonulopyranosid-2''-yl phosphate 
• 194665-66-2 allyl 2',3'-O,N⁴-triacetylcytidin-5'-yl methyl 5-[2-(acetoxy) acetamido]-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-β-D-glycero-D-galacto-2-nonulopyranosid-2''-yl phosphite 
• 194665-70-8 C₄₀H₅₃N₄O₂₅P 
• 40632-06-2 2',3'-O,N⁴-triacetylcytidine 
• 65-46-3 CYTIDINE 
• 194665-58-2 2',3'-O,N⁴-triacetyl-5'-tert-butyldiphenylsilyl cytidine 
• 175877-08-4 methyl 5-acetoxyacetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-β-D-galacto-2-nonulopyranosonate 
• 188786-02-9 2-allyl-2'-(2',3',N⁴-triacetyl-cytidin-5')-yl-N,N'-diisopropylphosphoramidite 
• 58479-65-5 5'-O-(tert-butyldiphenylsilyl)cytidine 
• 118865-39-7 methyl (5-acetoxyacetamido-4,7,8,9-tetra-O-acetyl-3,5-dideoxy-D-glycero-α-D-galacto-2-nonulopyranosyl chlorid)onate 
• 4710-95-6 D-mannosamine hydrochloride 

Relevant academic research and scientific papers

Efficient chemoenzymatic synthesis of O-linked sialyl oligosaccharides

The tumor associated Tn (GalNAcα(1-1)-Thr/Ser)- and T (Galβ(1-3)-GalNAcα(1-1)Thr/Ser)-antigens and their sialylated derivatives are present on the surface of many cancer cells. Preparative synthesis of these sialylated T- and Tn-structures has been achieved mainly from a chemical synthetic approach due to the lack of the required glycosyltransferases. We demonstrate a flexible and efficient chemoenzymatic approach for using recombinant sialyltransferases including a chicken GalNAcα2,6-sialyltransferase (chST6GalNAc I) and a porcine Galβ(1-3)GalNAcα-2,3-sialyltransferase (pST3Gal I). Using these enzymes, the common O-linked sialosides Neu5Acα(2-6)GalNAcα(1-1)Thr, Galβ(1-3)[Neu5Acα(2-6)] GalNAcα(1-1)Thr, Neu5Acα(2-3)Galβ(1-3)GalNAcα(1-1)Thr, and Neu5Acα(2-3)Galβ(1-3)[Neu5Acα(2-6)]GalNAcα(1-1)Thr were readily prepared at preparative scale. The chST6GalNAc I was found to require at least one amino acid (Thr/Ser) for optimal activity, and is thus an ideal catalyst for synthesis of synthetic glycopeptides and glycoconjugates with O-linked glycans.

Chemoenzymatic synthesis of CMP-sialic acid derivatives by a one-pot two-enzyme system: Comparison of substrate flexibility of three microbial CMP-sialic acid synthetases

Three microbial CMP-sialic acid synthetases were cloned from Neisseria meningitidis, Streptococcus agalactiae, and Escherichia coli, respectively. Their activities in the production of CMP-sialic acid analogs were compared by HPLC analysis. The N. meningitidis synthetase was used in the preparative synthesis of eight CMP-sialic acid derivatives in a one-pot two-enzyme system. Three C terminal His6-tagged recombinant microbial CMP-sialic acid synthetases [EC 2.7.7.43] cloned from Neisseria meningitidis group B, Streptococcus agalactiae serotype V, and Escherichia coli K1, respectively, were evaluated for their ability in the synthesis of CMP-sialic acid derivatives in a one-pot two-enzyme system. In this system, N-acetylmannosamine or mannose analogs were condensed with pyruvate, catalyzed by a recombinant sialic acid aldolase [EC 4.1.3.3] cloned from E. coli K12 to provide sialic acid analogs as substrates for the CMP-sialic acid synthetases. The substrate flexibility and the reaction efficiency of the three recombinant CMP-sialic acid synthetases were compared, first by qualitative screening using thin layer chromatography, and then by quantitative analysis using high performance liquid chromatography. The N. meningitidis synthetase was shown to have the highest expression level, the most flexible substrate specificity, and the highest catalytic efficiency among the three synthetases. Finally, eight sugar nucleotides, including cytidine 5′-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac) and its derivatives with substitutions at carbon-5, carbon-8, or carbon-9 of Neu5Ac, were synthesized in a preparative (100-200 mg) scale from their 5- or 6-carbon sugar precursors using the N. meningitidis synthetase and the aldolase.

Synthesis of CMP-sialic acid conjugates: Substrates for the enzymatic synthesis of natural and designed sialyl oligosaccharides

The syntheses of several congeners of CMP-NeuAc are described. These compounds are substrates for enzymatic glycosylation.