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      Structure and function of an acetyl xylan esterase (est2a) from the rumen bacterium Butyrivibrio proteoclasticus

      Till, Marisa; Goldstone, David C.; Attwood, Graeme T.; Moon, Christina D.; Kelly, Willam J.; Arcus, Vickery L.
      DOI
       10.1002/prot.24254
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      Till, 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.
      Permanent Research Commons link: https://hdl.handle.net/10289/7157
      Abstract
      Butyrivibrio 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.
      Date
      2013
      Type
      Journal Article
      Publisher
      Wiley
      Collections
      • Science and Engineering Papers [3069]
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