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Nat Commun. 2014 Jun 4;5:3975. doi: 10.1038/ncomms4975.

Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin.

Author information

  • 11] Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan [2] Advanced Low Carbon Technology Research and Development Program, Japan Science and Technology Agency, K's Gobancho 7, Gobancho, Chiyoda-ku, Tokyo 102-0076, Japan [3].
  • 21] Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan [2] Bio-AFM Frontier Research Center, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan [3].
  • 3Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
  • 4Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, 8050 Ikarashi-2, Nishi-ku, Niigata 950-2181, Japan.
  • 51] Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan [2] Department of Plant and Environmental New Resources, College of Life Sciences, Kyung Hee University, 1 Seocheon-dong, Giheung-ku, Yongin-si, Gyeonggi-do 446-701, Republic of Korea.
  • 6Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
  • 71] Department of Physics, Kanazawa University, Kakuma-machi, Kanazawa, Ishikawa 920-1192, Japan [2] Bio-AFM Frontier Research Center, College of Science and Engineering, Kanazawa University, Kakuma-machi, Kanazawa 920-1192, Japan.

Abstract

Processivity refers to the ability of synthesizing, modifying and degrading enzymes to catalyse multiple successive cycles of reaction with polymeric substrates without disengaging from the substrates. Since biomass polysaccharides, such as chitin and cellulose, often form recalcitrant crystalline regions, their degradation is highly dependent on the processivity of degrading enzymes. Here we employ high-speed atomic force microscopy to directly visualize the movement of two processive glycoside hydrolase family 18 chitinases (ChiA and ChiB) from the chitinolytic bacterium Serratia marcescens on crystalline β-chitin. The half-life of processive movement and the velocity of ChiA are larger than those of ChiB, suggesting that asymmetric subsite architecture determines both the direction and the magnitude of processive degradation of crystalline polysaccharides. The directions of processive movements of ChiA and ChiB are observed to be opposite. The molecular mechanism of the two-way traffic is discussed, including a comparison with the processive cellobiohydrolases of the cellulolytic system.

PMID:
24894873
[PubMed - in process]
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