The incorporation of tritium from tritium-enriched water into UDP-N-Acetylglucosamine and UDP-N-Acetyl Mannosamine catalyzed by UDP-N-Acetylglucosamine 2-Epimerase from Escherichia coli

Active site mutants of the “non-hydrolyz

Active site mutants of the “non-hydrolyzing” UDP-N-acetylglucosamine 2-epimerase from Escherichia coli

✍ Jomy Samuel; Martin E Tanner 📂 Article 📅 2004 🏛 Elsevier Science 🌐 English ⚖ 182 KB

The ''non-hydrolyzing'' bacterial UDP-N-acetylglucosamine 2-epimerase catalyzes the reversible interconversion of UDP-Nacetylglucosamine (UDP-GlcNAc) and UDP-N-acetylmannosamine (UDP-ManNAc). This homodimeric enzyme is allosterically activated by its substrate, UDP-GlcNAc, and it is thought that one