Structural characterization of Escherichia coli sialic acid synthase

Tzann Shun Hwang, Chih Hung Hung, Chin Fen Teo, Guan Ting Chen, Lee Shang Chang, Sung Fang Chen, Yu Ju Chen, Chun Hung Lin

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


Sialic acid synthase encoded by the neuB gene of Escherichia coli catalyzes the condensation of N-acetylmannosamine and phosphoenolpyruvate to form N-acetylneuraminic acid. This report demonstrates the first structural information on sialic acid synthase by CD MALDI-TOF and chemical cross-linking studies. Also a specific cleavage by endogenous protease(s) has been identified at Lys280 of the enzyme (40 kDa) by LC-MS and N-terminal sequencing analyses. The cleavage results in the formation of two inactive fragments of 33 and 7 kDa. The structural analysis indicates that the fragmentation is associated with a significant change of the enzyme from a tetrameric to trimeric form and alterations in both secondary and native quaternary structures.

Original languageEnglish
Pages (from-to)167-173
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2002
Externally publishedYes


  • Circular dichroism (CD)
  • Matrix-assisted laser desorption (MALDI)/ionization-time-of-flight (TOF)
  • N-Acetylneuraminic acid (NeuAc)
  • Sialic acid synthase
  • Subunit cross-linking

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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