Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Structural Analysis of ${\alpha}$-L-Arabinofuranosidase from Thermotoga maritima Reveals Characteristics for Thermostability and Substrate Specificity

  • Dumbrepatil, Arti (Department of Food Science and Technology, Chungbuk National University) ;
  • Park, Jung-Mi (Department of Food Science and Technology, Chungbuk National University) ;
  • Jung, Tae Yang (Medical Proteomics Research Center, Korea Research Institute of Biosciences and Biotechnology) ;
  • Song, Hyung-Nam (Medical Proteomics Research Center, Korea Research Institute of Biosciences and Biotechnology) ;
  • Jang, Myoung-Uoon (Department of Food Science and Technology, Chungbuk National University) ;
  • Han, Nam Soo (Department of Food Science and Technology, Chungbuk National University) ;
  • Kim, Tae-Jip (Department of Food Science and Technology, Chungbuk National University) ;
  • Woo, Eui Jeon (Medical Proteomics Research Center, Korea Research Institute of Biosciences and Biotechnology)
  • Received : 2012.08.20
  • Accepted : 2012.08.23
  • Published : 2012.12.28
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Abstract

An ${\alpha}$-L-arabinofuranosidase (TmAFase) from Thermotoga maritima MSB8 is a highly thermostable exo-acting hemicellulase that exhibits a relatively higher activity towards arabinan and arabinoxylan, compared with other glycoside hydrolase 51 family enzymes. In the present study, we carried out the enzymatic characterization and structural analysis of TmAFase. Tight domain associations found in TmAFase, such as an inter-domain disulfide bond (Cys306 and Cys476) in each monomer, a novel extended arm (amino acids 374-385) at the dimer interface, and total 12 salt bridges in the hexamer, may account for the thermostability of the enzyme. One of the xylan binding determinants (Trp96) was identified in the active site, and a region of amino acids (374-385) protrudes out forming an obvious wall at the substrate-binding groove to generate a cavity. The altered cavity shape with a strong negative electrostatic distribution is likely related to the unique substrate preference of TmAFase towards branched polymeric substrates.

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References

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