Structural and biochemical analyses of glycoside hydrolase family 26 β-mannanase from a symbiotic protist of the termite reticulitermes speratus

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Abstract

Background: Symbiotic protists of the termite gut contribute to lignocellulosic biomass degradation. Results: A novel protistan-mannanase efficiently degrades glucomannan and displays glucose/mannose binding properties when complexed with gluco-manno-oligosaccharide. Conclusion: Specific recognition and accommodation of glucose at the distal -subsites provides the structural basis for activity against glucomannan. Significance: The mechanism underlying heteropolysaccharide recognition by mannanase has been clarified. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.

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Tsukagoshi, H., Nakamura, A., Ishida, T., Touhara, K. K., Otagiri, M., Moriya, S., … Arioka, M. (2014). Structural and biochemical analyses of glycoside hydrolase family 26 β-mannanase from a symbiotic protist of the termite reticulitermes speratus. Journal of Biological Chemistry, 289(15), 10843–10852. https://doi.org/10.1074/jbc.M114.555383

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