Studies on enzymatic activity and conformational stability of muscle acylphosphatase mutated at conserved lysine residues

Protein Engineering

Volumn 11, Issue 7, 1998, Pages 557-561

  Chiti, Fabrizio ^a   Magherini, Francesca ^b   Taddei, Niccolò ^b   Ilardi, Claudia ^b   Stefani, Massimo ^b   Bucciantini, Monica ^b   Dobson, Christopher M ^a   Ramponi, Giampietro ^b  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Acylphosphatase; Catalytic mechanism; Circular dichroism; Conformational stability; Oligonucleotide directed mutagenesis

Indexed keywords

ACYLPHOSPHATASE; ENZYME INHIBITOR; ISOENZYME; LYSINE; MUTANT PROTEIN; SULFATE;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME KINETICS; ENZYME STABILITY; ERYTHROCYTE; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

EID: 0031927263     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/11.7.557     Document Type: Article

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