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pubmed-article:21212945pubmed:abstractTextL-Arabinose is the second most abundant pentose beside D-xylose and is found in the plant polysaccharides, hemicellulose and pectin. The need to find renewable carbon and energy sources has accelerated research to investigate the potential of L-arabinose for the development and production of biofuels and other bioproducts. Fungi produce a number of extracellular arabinanases, including ?-L-arabinofuranosidases and endo-arabinanases, to specifically release L-arabinose from the plant polymers. Following uptake of L-arabinose, its intracellular catabolism follows a four-step alternating reduction and oxidation path, which is concluded by a phosphorylation, resulting in D-xylulose 5-phosphate, an intermediate of the pentose phosphate pathway. The genes and encoding enzymes L-arabinose reductase, L-arabinitol dehydrogenase, L-xylulose reductase, xylitol dehydrogenase, and xylulokinase of this pathway were mainly characterized in the two biotechnological important fungi Aspergillus niger and Trichoderma reesei. Analysis of the components of the L-arabinose pathway revealed a number of specific adaptations in the enzymatic and regulatory machinery towards the utilization of L-arabinose. Further genetic and biochemical analysis provided evidence that L-arabinose and the interconnected D-xylose pathway are also involved in the oxidoreductive degradation of the hexose D-galactose.lld:pubmed
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pubmed-article:21212945pubmed:issn1432-0614lld:pubmed
pubmed-article:21212945pubmed:authorpubmed-author:SeibothBernha...lld:pubmed
pubmed-article:21212945pubmed:authorpubmed-author:MetzBenjaminBlld:pubmed
pubmed-article:21212945pubmed:issnTypeElectroniclld:pubmed
pubmed-article:21212945pubmed:volume89lld:pubmed
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pubmed-article:21212945pubmed:pagination1665-73lld:pubmed
pubmed-article:21212945pubmed:dateRevised2011-7-27lld:pubmed
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pubmed-article:21212945pubmed:articleTitleFungal arabinan and L-arabinose metabolism.lld:pubmed
pubmed-article:21212945pubmed:affiliationResearch Area Gene Technology and Applied Biochemistry, Institute of Chemical Engineering, Vienna University of Technology, Wien, Austria. bseiboth@mail.tuwien.ac.atlld:pubmed
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