The catalytic mechanism and unique low pH optimum of Caldicellulosiruptor bescii family 3 pectate lyase

The unique active site of the Caldicellulosiruptor bescii family 3 pectate lyase (PL3) enzyme has been thoroughly characterized using a series of point mutations, X-ray crystallography, pK (a) calculations and biochemical assays. The X-ray structures of seven PL3 active-site mutants, five of them in...

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Detalhes bibliográficos
Publicado no:Acta Crystallogr D Biol Crystallogr
Main Authors: Alahuhta, Markus, Taylor, Larry E., Brunecky, Roman, Sammond, Deanne W., Michener, William, Adams, Michael W. W., Himmel, Michael E., Bomble, Yannick J., Lunin, Vladimir
Formato: Artigo
Idioma:Inglês
Publicado em: International Union of Crystallography 2015
Assuntos:
Research Papers
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4556314/
https://ncbi.nlm.nih.gov/pubmed/26327384
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1399004715013760
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