Reciprocal effects of substitutions at the subunit interfaces in hexameric pyrophosphatase of Escherichia coli. Dimeric and monomeric forms of the enzyme

Journal of Biological Chemistry

Volumn 274, Issue 48, 1999, Pages 33898-33904

  Salminen, Anu ^a   Efimova, Irina S ^b   Parfenyev, Alexey N ^b   Magretova, Natalia N ^b   Mikalahti, Katja ^a   Goldman, Adrian ^a   Baykov, Alexander A ^b   Lahti, Reijo ^a  

^a UNIVERSITY OF TURKU   (Finland)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GLUTAMINE; HISTIDINE; INORGANIC PYROPHOSPHATASE; MAGNESIUM ION; MONOMER; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; ASPARTIC ACID; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; ENZYME STABILITY; ESCHERICHIA COLI; GLUTAMIC ACID; GLUTAMINE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; MAGNESIUM COMPOUNDS; PROTEIN STRUCTURE, QUATERNARY; PYROPHOSPHATASES; SUBSTRATE SPECIFICITY; TEMPERATURE; TYROSINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033607547     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.48.33898     Document Type: Article

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