Mechanism by which metal cofactors control substrate specificity in pyrophosphatase

Biochemical Journal

Volumn 367, Issue 3, 2002, Pages 901-906

  Zyryanov, Anton B ^a   Shestakov, Alexander S ^a   Lahti, Reijo ^a   Baykov, Alexander A ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

ATP; ATPase; P1; Tripolyphosphate

Indexed keywords

CATALYSIS; ENZYMES; ESCHERICHIA COLI; HYDROLYSIS; PHOSPHATES; PHYSIOLOGY; TRANSITION METALS; WATER;

METAL COFACTORS;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; COBALT; FUNGAL ENZYME; INORGANIC PYROPHOSPHATASE; LIVER ENZYME; MAGNESIUM; MANGANESE; METAL; TRANSITION ELEMENT; TRIPOLYPHOSPHATE; WATER; ZINC;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR SIZE; NONHUMAN; PRIORITY JOURNAL; RAT; SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; CATALYSIS; HYDROLYSIS; METALS; PROTEIN BINDING; PYROPHOSPHATASES; SUBSTRATE SPECIFICITY;

ANIMALIA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE; STREPTOCOCCUS MUTANS;

EID: 0036845883     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020880     Document Type: Article

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