Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: Biased distribution of acidic residues and importance of Asp37 for catalysis at low pH

Protein Engineering

Volumn 11, Issue 12, 1998, Pages 1121-1128

  Fushinobu, Shinya ^a   Ito, Kiyoshi ^b   Konno, Michiko ^c   Wakagi, Takayoshi ^a   Matsuzawa, Hiroshi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b NATIONAL RESEARCH INSTITUTE OF BREWING   (Japan)

^c OCHANOMIZU UNIVERSITY   (Japan)

Author keywords

Acid stability; Aspergillus kawachii; Low pH optimum; X ray crystallography; Xylanase

Indexed keywords

ASPARTIC ACID; FUNGAL PROTEIN; MUTANT PROTEIN; XYLAN ENDO 1,3 BETA XYLOSIDASE;

ACIDITY; AMINO ACID COMPOSITION; ARTICLE; ASPERGILLUS; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PH; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

EID: 0032407988     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/11.12.1121     Document Type: Article

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