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Primary structure and expression analysis of humanUDP‐N‐acetyl‐glucosamine‐2‐epimerase/N‐acetylmannosamine kinase,the bifunctional enzyme in neuraminic acid biosynthesis 1
Author(s) -
Lothar Lucka,
Michael Krause,
Kerstin Danker,
Werner Reutter,
Rüdiger Horstkorte
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00837-6
Subject(s) - phosphofructokinase 2 , biochemistry , neuraminic acid , biosynthesis , enzyme , glucosamine , glycosyltransferase , sialic acid , complementary dna , biology , peptide sequence , cytosol , glycoprotein , microbiology and biotechnology , chemistry , gene
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-acetyl-glucosamine-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.