The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli

FEBS Letters

Volumn 580, Issue 30, 2006, Pages 6763-6768

  Ramazzotti, Matteo ^a   Parrini, Claudia ^a   Stefani, Massimo ^a   Manao, Giampaolo ^a   Degl'Innocenti, Donatella ^a  

^a UNIVERSITY OF FLORENCE   (Italy)

Author keywords

Acylphosphatase; Disulfide bridge; Enzyme activity; Escherichia coli; Prokaryotes; Protein denaturation

Indexed keywords

ACYLPHOSPHATASE; DISULFIDE; RECOMBINANT ENZYME;

ARTICLE; BACTERIAL GENE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MESOPHYLL; NONHUMAN; OPEN READING FRAME; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN EXPRESSION; REAL TIME POLYMERASE CHAIN REACTION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

ACID ANHYDRIDE HYDROLASES; AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; CYSTEINE; DISULFIDES; ENZYME STABILITY; ESCHERICHIA COLI; HUMANS; ISOENZYMES; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN DENATURATION; SEQUENCE ALIGNMENT; TEMPERATURE; THERMODYNAMICS; UREA;

ESCHERICHIA COLI; PROKARYOTA;

EID: 33845460350     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.11.033     Document Type: Article

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