title: Identification of the amino acid residues affecting the catalytic pocket of the Sulfolobus solfataricus signature amidase.
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.
authors.affiliation: Dipartimento di Ingegneria e Scienza dell'Informazione, University of Trento, Via Sommarive 14, 38100 Trento (TN), Italy.
authors.forename: Cilia
authors.initials: C
authors.lastname: Elisa
authors.forename: Ammendola
authors.initials: A
authors.lastname: Sergio
mesh_terms: D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry*; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001120:Arginine / Q000737:chemistry; D001185:Artificial Intelligence; D001224:Aspartic Acid / Q000737:chemistry; D055162:Biocatalysis; D020134:Catalytic Domain; D019295:Computational Biology / Q000379:methods; D017124:Conserved Sequence; D008239:Lysine / Q000737:chemistry; D008958:Models, Molecular; D016296:Mutagenesis; D050505:Mutant Proteins / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D013379:Substrate Specificity; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics
chemical_list: D000596:Amino Acids; D019843:Archaeal Proteins; D050505:Mutant Proteins; D011994:Recombinant Proteins; D001224:Aspartic Acid; D001120:Arginine; D000581:Amidohydrolases; C019665:amidase; D008239:Lysine