Identification of the amino acid residues affecting the catalytic pocket of the Sulfolobus solfataricus signature amidase.
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.
Elisa
Cilia
C
Dipartimento di Ingegneria e Scienza dell'Informazione, University of Trento, Via Sommarive 14, 38100 Trento (TN), Italy.
Sergio
Ammendola
A
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
D000596:Amino Acids; D019843:Archaeal Proteins; D050505:Mutant Proteins; D011994:Recombinant Proteins; D001224:Aspartic Acid; D001120:Arginine; D000581:Amidohydrolases; C019665:amidase; D008239:Lysine