A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Engineering a new magnesium binding site in the subunit contact region of Escherichia coli inorganic pyrophosphatase
Tekijät: Parfenyev AN, Salminen A, Baykov AA, Lahti R
Kustantaja: CONSULTANTS BUREAU
Julkaisuvuosi: 2000
Journal: Биохимия / Biochemistry
Tietokannassa oleva lehden nimi: BIOCHEMISTRY-MOSCOW
Lehden akronyymi: BIOCHEMISTRY-MOSCOW+
Vuosikerta: 65
Numero: 3
Aloitussivu: 388
Lopetussivu: 392
Sivujen määrä: 5
ISSN: 0006-2979
Tiivistelmä
Three Gln-80 residues belonging to different subunits of homohexameric Escherichia coli pyrophosphatase are separated by only one water molecule to which they are hydrogen bonded. Substitution of Glu for Gln-80 stabilizes quaternary structure of the enzyme but has only a small effect on enzyme activity. The substitution stimulates Mg2+ binding and changes the appearance of the Mg2+ concentration dependence of the rate constant for the trimer --> hexamer transition. These data suggest that a new Mg2+ binding site is formed in the intersubunit contact region as a result of the substitution. Three-dimensional modeling of the mutated protein showed that a chelate complex might form involving two of the three Glu-80 residues.
Three Gln-80 residues belonging to different subunits of homohexameric Escherichia coli pyrophosphatase are separated by only one water molecule to which they are hydrogen bonded. Substitution of Glu for Gln-80 stabilizes quaternary structure of the enzyme but has only a small effect on enzyme activity. The substitution stimulates Mg2+ binding and changes the appearance of the Mg2+ concentration dependence of the rate constant for the trimer --> hexamer transition. These data suggest that a new Mg2+ binding site is formed in the intersubunit contact region as a result of the substitution. Three-dimensional modeling of the mutated protein showed that a chelate complex might form involving two of the three Glu-80 residues.
Turun yliopiston Tutkimustietojärjestelmän portaali