Characterization of mutants of Sulfolobus solfataricus signature amidase able to hydrolyse R-ketoprofen amide.
The amidase from Sulfolobus solfataricus enantioselectively hydrolyzes S-ketoprofen amide to its corresponding acid. We identify three independent SsAH mutants that hydrolyze R-ketoprofen amide and built computational models of their three-dimensional structure. Interestingly the mutations do not specifically affect residues near the active site, or directly interacting with the substrate.
Giordano
Cesare
C
CNR - Instituto di Chimica Biomolecolare, "Sapienza" University of Rome, Rome, Italy.
Ammendola
Sergio
S
D000581:Amidohydrolases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D020134:Catalytic Domain; D006868:Hydrolysis; D007660:Ketoprofen / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009154:Mutation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D013237:Stereoisomerism; D013379:Substrate Specificity; D048229:Sulfolobus solfataricus / Q000201:enzymology* / Q000235:genetics
D019843:Archaeal Proteins; D007660:Ketoprofen; D000581:Amidohydrolases; C019665:amidase