Identification of the amino acid residues affecting the catalytic pocket of the Sulfolobus solfataricus signature amidase

Protein Pept Lett. 2010 Feb;17(2):146-50. doi: 10.2174/092986610790226021.

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.

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism*
  • Amino Acid Sequence
  • Amino Acids / chemistry*
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism*
  • Arginine / chemistry
  • Artificial Intelligence
  • Aspartic Acid / chemistry
  • Biocatalysis
  • Catalytic Domain*
  • Computational Biology / methods
  • Conserved Sequence
  • Lysine / chemistry
  • Models, Molecular
  • Mutagenesis
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Sulfolobus solfataricus / enzymology*
  • Sulfolobus solfataricus / genetics

Substances

  • Amino Acids
  • Archaeal Proteins
  • Mutant Proteins
  • Recombinant Proteins
  • Aspartic Acid
  • Arginine
  • Amidohydrolases
  • amidase
  • Lysine