Substitutions of Thr-103-Ile and Trp-138-Gly in amidase from Pseudomonas aeruginosa are responsible for altered kinetic properties and enzyme instability

Applied Biochemistry and Biotechnology - Part B Molecular Biotechnology

Volumn 17, Issue 3, 2001, Pages 201-212

  Karmali, A ^a   Pacheco, R ^a   Tata, R ^a   Brown, P ^a  

^a INSTITUTO SUPERIOR DE ENGENHARIA DE LISBOA   (Portugal)

Author keywords

Altered kinetic properties; Enzyme instability; Ph1 mutant amidase; Pseudomonas aeruginosa; Site directed mutagenesis; Wild type amidase

Indexed keywords

ACETAMIDE; ACETANILIDE; ACRYLAMIDE; AMIDASE; GLYCINE; ISOLEUCINE; MONOCLONAL ANTIBODY; SEPHAROSE; THREONINE; TRYPTOPHAN;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BACTERIUM MUTANT; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STABILITY; EXPRESSION VECTOR; GEL FILTRATION CHROMATOGRAPHY; NONHUMAN; PH; POLYMERASE CHAIN REACTION; PSEUDOMONAS AERUGINOSA; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS;

AMIDOHYDROLASES; ENZYME-LINKED IMMUNOSORBENT ASSAY; GLYCINE; HYDROGEN-ION CONCENTRATION; ISOLEUCINE; KINETICS; MUTAGENESIS, SITE-DIRECTED; MUTATION; PLASMIDS; POLYMERASE CHAIN REACTION; PSEUDOMONAS AERUGINOSA; TEMPERATURE; THREONINE; TRYPTOPHAN; UREA;

BACTERIA (MICROORGANISMS); PROKARYOTA; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 0034966202     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:17:3:201     Document Type: Article

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