Engineering of Pseudomonas aeruginosa lipase by directed evolution for enhanced amidase activity: mechanistic implication for amide hydrolysis by serine hydrolases

A lipase from Pseudomonas aeruginosa was subjected to directed evolution for increased amidase activity to probe the catalytic mechanism of serine hydrolases for the hydrolysis of amides. Random mutagenesis combined with saturation mutagenesis for all the amino acid residues at the substrate-binding...

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Veröffentlicht in:	Protein engineering, design and selection design and selection, 2007-07, Vol.20 (7), p.339-346
Hauptverfasser:	Nakagawa, Yuichi, Hasegawa, Atsuko, Hiratake, Jun, Sakata, Kanzo
Format:	Artikel
Sprache:	eng
Schlagworte:	amidase activity Amidohydrolases - metabolism Amino Acid Sequence Binding Sites catalytic triad directed evolution Directed Molecular Evolution - methods Kinetics leaving group protonation Lipase - genetics Lipase - metabolism Models, Molecular Molecular Sequence Data Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Pseudomonas aeruginosa - genetics Pseudomonas aeruginosa lipase Serine Endopeptidases - metabolism
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