Substrate promiscuity of n-acetylhexosamine 1-kinases

Yanhong Li, Hai Yu, Yi Chen, Kam Lau, Li Cai, Hongzhi Cao, Vinod Kumar Tiwari, Jingyao Qu, Vireak Thon, Peng George Wang, Xi Chen

Research output: Contribution to journalArticlepeer-review

50 Scopus citations


N-Acetylhexosamine 1-kinase (NahK) catalyzes the direct addition of a phosphate from adenosine 5'-triphosphate (ATP) to the anomeric position of N-acetylhexosamine and shows similar activity towards N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc). Herein we report the cloning, characterization, and substrate specificity studies of two NahKs from Bifidobacterium infantis ATCC15697 and Bifidobacterium longum ATCC55813, respectively. A new capillary electrophoresis assay method has been developed for enzyme activity assays. Both enzymes have a good expression level in E. coli (180-185 mg/L culture) and can tolerate diverse modifications at C2 of GlcNAc and GalNAc. Various GlcNAc derivatives with C6, both C2 and C6, as well as both C2 and C3 modifications are tolerable substrates for the newly cloned NahKs. Quite interestingly, despite of their low activities toward glucose and galactose, the activities of both NahKs are much higher for mannose and some of its C2, C4, and C6 derivatives. These NahKs are excellent catalysts for enzymatic and chemoenzymatic synthesis of carbohydrates.

Original languageEnglish (US)
Pages (from-to)6396-6407
Number of pages12
Issue number8
StatePublished - Aug 2011


  • Mannose
  • N-acetylgalactosamine
  • N-acetylglucosamine
  • N-acetylhexosamine 1-kinase
  • Substrate specificity

ASJC Scopus subject areas

  • Organic Chemistry


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