Journal
FEBS LETTERS
Volume 583, Issue 9, Pages 1457-1462Publisher
WILEY
DOI: 10.1016/j.febslet.2009.03.057
Keywords
alpha-Glucuronidase; Glycoside hydrolase; Xylanolytic enzyme; Pichia stipitis
Funding
- Slovak Research and Development Agency APVV [SK-ZA-000507]
- National Research Foundation in South Africa
- Slovak
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Investigation of the xylanolytic enzyme system of the xylose-fermenting yeast Pichia stipitis resulted in the discovery of an extracellular alpha-glucuronidase efficiently debranching hardwood glucuronoxylan. This activity is not exhibited by more extensively investigated alpha-glucuronidases of glycoside hydrolase (GH) family 67, operating on substrates in which the uronic acid is linked to the non-reducing xylopyranosyl residues of main chain fragments. The N-terminus of the purified enzyme corresponded exactly to the P. stipitis gene ABN67901 coding for a protein of unknown function. BLAST search revealed the presence of similar genes in genomes of other microorganisms. These results lead to the emergence of a new family of alpha-glucuronidases. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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