Literature DB >> 19344716

A novel family of hemicellulolytic alpha-glucuronidase.

Olena Ryabova1, Mária Vrsanská, Satoshi Kaneko, Willem H van Zyl, Peter Biely.   

Abstract

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.

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Year:  2009        PMID: 19344716     DOI: 10.1016/j.febslet.2009.03.057

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  22 in total

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