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Updated: Aug 14, 2026

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
Published on: November 25, 2017
Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes
Abstract:
The enzymes UDP-N-acetylglucosamine pyrophosphorylase, UDP-N-acetylglucosamine 2-epimerase, N-acetylmannosamine kinase, N-acetylglucosamine kinase and N-acetylglucosamine 2-epimerase, which are involved in the metabolism of N-acetylneuraminic acid, were studied in rat with regard to their subcellular localization and tissue distribution. The subcellular distribution studies in liver indicated that the enzymes are localized in the soluble cell fraction. In other tissues the comparison of enzyme activities in homogenates with that in high-speed supernatants led to a similar conclusion. UDP-N-acetylglucosamine pyrophosphorylase, N-acetylglucosamine kinase and N-acetylglucosamine 2-epimerase were detected in almost all tissues studied. UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase, two enzymes considered to be key enzymes in the N-acetylneuraminic acid biosynthesis, were detected only in sialoglycoprotein-secreting tissues, i.e. liver, salivary gland and intestinal mucosa. The low activity of the key enzymes in other tissues suggests that the biosynthetic pathway of N-acetylneuraminic acid is not the same in various tissues.
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