Distinct structure and activity recoveries reveal differences in metal binding between mammalian and Escherichia coli alkaline phosphatases

Biochemical Journal

Volumn 392, Issue 2, 2005, Pages 407-415

  Zhang, Le ^a   Buchet, René ^a   Azzar, Gérard ^a  

^a UNIVERSITÉ LYON 1   (France)

Author keywords

Activity recovery; Alkaline phosphatase; Apo enzyme; Ion binding; Structure recovery

Indexed keywords

AMINO ACIDS; DIMERS; ESCHERICHIA COLI; IONS; MAGNESIUM PRINTING PLATES; MONOMERS; SENSITIVITY ANALYSIS; ZINC;

ACTIVITY RECOVERY; ALKALINE PHOSPHATASE; APO-ENZYME; ION-BINDING; STRUCTURE RECOVERY;

ENZYMES;

ALKALINE PHOSPHATASE; AMINO ACID; APOENZYME; DIMER; METAL;

AMINO ACID SEQUENCE; ARTICLE; CHELATION; DIMERIZATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; MAMMAL CELL; METAL BINDING; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

ALKALINE PHOSPHATASE; ANIMALS; BINDING SITES; CATTLE; ESCHERICHIA COLI; MAGNESIUM; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; ZINC;

BOVINAE; ESCHERICHIA COLI; MAMMALIA;

EID: 29144531187     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20050509     Document Type: Article

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