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

33 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

Bibliographical note

Funding Information:
We thank Dr. H.S. Lee, K.J. Kim, and K.H. Kim for their kind assistance with the data collection using beamlines 4A and 6C of the Pohang Light Source, Korea. This study was supported by the Korea Science and Engineering Foundation. [R01-2007-000-20072-0 (2009)]. K.H. Nam is supported by the BK21 program.


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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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