Structural insights into the substrate recognition properties of β-glucosidase

Ki Hyun Nam, Min Woo Sung, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)


β-Glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that β-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of β-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of β-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of β-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of β-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of β-glucosidase.

Original languageEnglish
Pages (from-to)1131-1135
Number of pages5
JournalBiochemical and biophysical research communications
Issue number1
Publication statusPublished - 2010 Jan 1


  • Catalysis processing
  • Intermediate state
  • Steric hindrance
  • Substrate specificity
  • β-Glucosidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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