Linked Life Data

12374797

Source:http://linkedlifedata.com/resource/pubmed/id/12374797

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pubmed-article:12374797pubmed:abstractTextA novel oligoxyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase (OXG-RCBH), with a molecular mass of 97 kDa and a pI of 6.1, was isolated from the fungus Geotrichum sp. M128. Analysis of substrate specificity using various xyloglucan oligosaccharide structures revealed that OXG-RCBH had exoglucanase activity. It recognized the reducing end of oligoxyloglucan and released two glucosyl residue segments from the main chain. The full-length cDNA encoding OXG-RCBH was cloned and sequenced, and it had a 2436-bp open reading frame encoding an 812amino acid protein. The deduced protein showed approximately 35% identity to members of glycoside hydrolase family 74. The cDNA encoding OXG-RCBH was then expressed in Escherichia coli. Although the recombinant protein was expressed as an inclusion body, renaturation was successful, and enzymatically active recombinant OXG-RCBH was obtained.lld:pubmed
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pubmed-article:12374797pubmed:authorpubmed-author:YaoiKatsuroKlld:pubmed
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pubmed-article:12374797pubmed:pagination48276-81lld:pubmed
pubmed-article:12374797pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:12374797pubmed:year2002lld:pubmed
pubmed-article:12374797pubmed:articleTitlePurification, characterization, cloning, and expression of a novel xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase.lld:pubmed
pubmed-article:12374797pubmed:affiliationInstitute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Tsukuba Central 6, 1-1-1 Higashi, Ibaraki 305-8566, Japan. k-yaoi@aist.go.jplld:pubmed
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