Primary structure and expression analysis of human UDP- N-acetyl-glucosamine-2-epimerase/ N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis

• Published in: FEBS letters Vol. 454; no. 3; pp. 341 - 344
• Main Authors: Lucka, Lothar, Krause, Matthias, Danker, Kerstin, Reutter, Werner, Horstkorte, Rüdiger
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 09.07.1999
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Carbohydrate Epimerases - genetics; Carbohydrate Epimerases - metabolism; Cloning, Molecular; DNA, Complementary - analysis; DNA, Complementary - genetics; Escherichia coli Proteins; Humans; Molecular Sequence Data; N-Acetylneuraminic Acid - biosynthesis; Neuraminic acid biosynthesis; Phosphotransferases (Alcohol Group Acceptor) - genetics; Phosphotransferases (Alcohol Group Acceptor) - metabolism; Rats; Sequence Alignment; Tissue expression; UDP- N-acetylglucosamine-2-epimerase/ N-acetylmannosamine kinase; Neuraminic acid biosynthesis; UDP- N-acetylglucosamine-2-epimerase/ N-acetylmannosamine kinase; Tissue expression
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)00837-6

N-Acetylneuraminic acid is a main constituent of glycoproteins and gangliosides. In many membrane-bound receptors it is the target for external stimuli. The key enzyme for its biosynthesis is the bifunctional enzyme UDP- N-acetylglucosamine-2-epimerase/ N-acetylmannosamine kinase, catalysing the first two steps of the biosynthesis in the cytosol. The rat enzyme was previously isolated and characterised. In this report we present the corresponding human cDNA sequence, compare it with the primary structure of the rodent enzyme, and report the analysis of its expression in different human tissues and cell lines.