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The membrane-bound α-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan

Lookup NU author(s): Tibor Nagy, Dr Kaveh Emami, Emeritus Professor Harry Gilbert

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Abstract

The microbial degradation of xylan is a key biological process. Hardwood 4-O-methyl-D-glucuronoxylans are extensively decorated with 4-O-methyl-D-glucuronic acid, which is cleaved from the polysaccharides by α-glucuronidases. In this report we describe the primary structures of the α-glucuronidase from Cellvibrio mixtus (C. mixtus GlcA67A) and the α-glucuronidase from Pseudomonas cellulosa (P. cellulosa GlcA67A) and characterize P. cellulosa GlcA67A. The primary structures of C. mixtus GlcA67A and P. cellulosa GlcA67A, which are 76% identical, exhibit similarities with α-glucuronidases in glycoside hydrolase family 67. The membrane-associated pseudomonad α-glucuronidase released 4-O-methyl-D-glucuronic acid from 4-O-methyl-D-glucuronoxy-looligosaccharides but not from 4-O-methyl-D-glucuronoxylan. We propose that the role of the glucuronidase, in combination with cell-associated xylanases, is to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers.

Publication metadata

Author(s): Nagy T, Emami K, Fontes CMGA, Ferreira LMA, Humphry DR, Gilbert HJ

Publication type: Article

Publication status: Published

Journal: Journal of Bacteriology

Year: 2002

Volume: 184

Issue: 17

Pages: 4925-4929

ISSN (print): 0021-9193

ISSN (electronic): 1098-5530

Publisher: American Society for Microbiology

URL: http://dx.doi.org/10.1128/JB.184.17.4925-4929.2002

DOI: 10.1128/JB.184.17.4925-4929.2002

PubMed id: 12169619

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