Show simple item record  

dc.contributor.authorTill, Marisa
dc.contributor.authorGoldstone, David C.
dc.contributor.authorAttwood, Graeme T.
dc.contributor.authorMoon, Christina D.
dc.contributor.authorKelly, Willam J.
dc.contributor.authorArcus, Vickery L.
dc.identifier.citationTill, M., Goldstone, D. C., Attwood, G. T., Moon, C. D., Kelly, W. J., & Arcus, V. L. (2013). Structure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticus. Proteins: Structure, Function, and Bioinformatics, 81(5), 911-917.en_NZ
dc.description.abstractButyrivibrio proteoclasticus is a significant component of the microbial population of the rumen of dairy cattle. It is a xylan-degrading organism whose genome encodes a large number of open reading frames annotated as fibre-degrading enzymes. We have determined the three-dimensional structure of Est2A, an acetyl xylan esterase from B. proteoclasticus, at 2.1 Å resolution, along with the structure of an inactive mutant (H351A) at 2.0 Å resolution. The structure reveals two domains - a C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures. The structures are accompanied by experimentally determined enzymatic parameters against two model substrates, para-nitrophenyl acetate and para-nitrophenyl butyrate. The suite of fibre-degrading enzymes produced by B. proteoclasticus provides a rich source of new enzymes of potential use in industrial settings.en_NZ
dc.relation.ispartofProteins: Structure, Function, and Bioinformatics
dc.titleStructure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticusen_NZ
dc.typeJournal Articleen_NZ

Files in this item


There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record