Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 6, 2007, Pages 679-687

  Ásgeirsson, Bjarni ^a   Adalbjörnsson, Björn Vidar ^a   Gylfason, Gudjón Andri ^a  

^a UNIVERSITY OF ICELAND   (Iceland)

Author keywords

Catalytic efficiency; Cold adaptation; Cysteine; Disulfide bond; Site directed mutagenesis

Indexed keywords

ALKALINE PHOSPHATASE; CYSTEINE; DISULFIDE; SERINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CIRCULAR DICHROISM; COLD ACCLIMATIZATION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STABILITY; NONHUMAN; PREDICTION; PRIORITY JOURNAL; REACTION TIME; SEQUENCE ANALYSIS; THERMOSTABILITY; VIBRIO;

ALKALINE PHOSPHATASE; BINDING SITES; CATALYSIS; COLD; DISULFIDES; ENZYME STABILITY; ESCHERICHIA COLI; HEAT; KINETICS; MODELS, MOLECULAR; MUTATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; VIBRIO;

ESCHERICHIA COLI; EUKARYOTA; VERTEBRATA; VIBRIO SP.;

EID: 34249882805     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.03.016     Document Type: Article

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