Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library

Ki Hyun Nam, Soo Jin Kim, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


Degradation of polysaccharides by cellulases and xylanases plays an important role in the carbon cycle, but only occurs in plant cell walls, a few bacteria and some animals. This process is also critical in processes such as biomass degradation and fuel production in the conversion cycles of cellulosic biomass. The enzyme CelM2 is bifunctional, because it is able to effectively hydrolyze barley glucan and xylan. Here, we show the crystal structure of the bifunctional enzyme CelM2, isolated from a metagenome library, and describe the sequence information and structure of its two domains. We believe that CelM2 is attractive as an industrial enzyme and that the structural results presented herein provide insights that are relevant to the genetic engineering of multifunctional enzymes.

Original languageEnglish
Pages (from-to)183-186
Number of pages4
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 2009 May 29

Bibliographical note

Funding Information:
We thank Dr. H.S. Lee and his staff for assistance during data collection at Beamline 4A of the Pohang Light Source, Korea. This work was supported by the Korea Institute of Environmental Science and Technology (2008-02001-0062-0) and the National Academy of Agricultural Science RDA. K.H. Nam is supported by the BK21 program.

Copyright 2009 Elsevier B.V., All rights reserved.


  • Bifunctional enzyme
  • CelM2
  • Glucanase
  • Glucanase-xylanase
  • Xylanase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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