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2000
Volume 17, Issue 2
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

36 mutants of the Sulfolobus solfataricus amidase were analyzed by comparing biochemical data to structural data obtained by a learning machine. The analysis shows that beside well known catalytic residues, amino acid residues Arg197, Lys209 and Asp228 are important for the catalytic activity of the signature thermophilic amidase.

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/content/journals/ppl/10.2174/092986610790226021
2010-02-01
2025-05-25
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/content/journals/ppl/10.2174/092986610790226021
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  • Article Type:
    Research Article
Keyword(s): amidase; FRAP; Functional residues; machine learning; SVM
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