Literature DB >> 16820683

Crystallization and preliminary crystallographic analysis of the family GH78 alpha-L-rhamnosidase RhaB from Bacillus sp. GL1.

Zhongli Cui1, Yukie Maruyama, Bunzo Mikami, Wataru Hashimoto, Kousaku Murata.   

Abstract

Alpha-L-rhamnosidases play important roles in the metabolism of plant cell walls, glycosides and bacterial biofilms. This enzyme is also used industrially for debittering citrus fruits by releasing rhamnose from the plant flavonoid naringin. Bacillus sp. GL1 alpha-L-rhamnosidase (RhaB) is a member of glycoside hydrolase (GH) family 78. Native and selenomethionine-derivative enzymes were crystallized at 293 K by hanging-drop vapour diffusion with polyethylene glycol 8000 as a precipitant. This is the first report of the crystallization of a family GH78 enzyme.

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Year:  2006        PMID: 16820683      PMCID: PMC2242939          DOI: 10.1107/S174430910601904X

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  13 in total

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Review 8.  Gellan gum.

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Journal:  Arch Biochem Biophys       Date:  2003-07-15       Impact factor: 4.013

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  2 in total

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