Effects of active site mutations on the metal binding affinity, catalytic competence, and stability of the family II pyrophosphatase from Bacillus subtilis

Biochemistry

Volumn 44, Issue 10, 2005, Pages 4004-4010

  Halonen, Pasi ^a,d   Tammenkoski, Marko ^a   Niiranen, Laila ^a   Huopalahti, Sauli ^a   Parfenyev, Alexey N ^b   Goldman, Adrian ^c   Baykov, Alexander ^b   Lahti, Reijo ^a  

^a UNIVERSITY OF TURKU   (Finland)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c UNIVERSITY OF HELSINKI   (Finland)

^d VTT TECHNICAL RESEARCH CENTRE OF FINLAND   (Finland)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACTERIA; BINDING ENERGY; CATALYSIS; MANGANESE; POTASSIUM; SENSITIVITY ANALYSIS; THERMODYNAMIC STABILITY;

BACILLUS SUBTILIS; INORGANIC PYROPHOSPHATASES; METAL BINDING AFFINITY; MUTATIONS;

ENZYMES;

ASPARTIC ACID; DIMER; GLUTAMINE; HISTIDINE; INORGANIC PYROPHOSPHATASE; MAGNESIUM; MANGANESE; PROTEIN SUBUNIT;

ARTICLE; BACILLUS SUBTILIS; BINDING AFFINITY; CATALYSIS; ENZYME STABILITY; ENZYME STRUCTURE; GENE MUTATION; METAL BINDING; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; STEADY STATE; THERMAL ANALYSIS; THERMOSTABILITY;

AMINO ACID SUBSTITUTION; BACILLUS SUBTILIS; BINDING SITES; CATALYTIC DOMAIN; CATIONS, DIVALENT; CONSERVED SEQUENCE; DIMERIZATION; ENZYME STABILITY; INORGANIC PYROPHOSPHATASE; KINETICS; MAGNESIUM; MANGANESE; MUTAGENESIS, SITE-DIRECTED; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; THERMODYNAMICS;

BACILLUS SUBTILIS;

EID: 14844342751     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047926u     Document Type: Article

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