Interrupted catalytic domain structures in xylanases from two distantly related strains of Prevotella ruminicola |
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| Affiliation: | 1. School of Psychology, Université Laval, Canada;2. Institute of Genetic, Neurobiological, and Social Foundations of Child Development, Tomsk State University, Tomsk, Russian Federation;3. Department of Psychoeducation, Université de Sherbrooke, Canada;4. Department of Psychology, University of London, Goldsmiths, England, United Kingdom;5. Laboratory for Cognitive Investigations and Behavioural Genetics, Tomsk State University, Russian Federation;6. Department of Psychoeducation, Université de Montréal, Montréal, Canada;7. Department of Psychiatry, Université de Montréal, Canada;8. CHU Ste-Justine Research Center, Université de Montréal, Montréal, Canada;9. Department of Pediatrics and Psychology, Université de Montréal, Canada;10. School of Public Health, Physiotherapy and Population Sciences, University College Dublin, Ireland |
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| Abstract: | Two xylanases from the rumen anaerobic bacterium Prevotella ruminicola were found to possess highly unusual structures in which family 10 catalytic domains are interrupted by unrelated sequences. XynC from P. ruminicola B14 carries a 160 amino-acid insertion, while a P. ruminicola D31d xylanase carries an unrelated region of 280 amino acids, containing an imperfect 130 amino-acid duplication. Both regions of family 10 similarity were shown to be essential for activity of the D31d enzyme. |
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