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Cold lability of the mutant forms of Escherichia coli inorganic pyrophosphatase
Author(s) -
Velichko Irina V.,
Volk Sergej E.,
Dudarenkov Valerij Yu.,
Magretova Natalia N.,
Chernyak Viktor Ya.,
Goldman Adrian,
Cooperman Barry S.,
Lahti Reijo,
Baykov Alexander A.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00003-r
Subject(s) - lability , inorganic pyrophosphatase , escherichia coli , mutant , enzyme , pyrophosphatase , chemistry , biochemistry , pyrophosphate , gene
The variants of Escherichia coli pyrophosphatase carrying the substitutions Glu20 → Asp, His136 → Gln or His140 → Gln are inactivated, in contrast to the wild‐type enzyme, at temperatures below 25°C: their activity measured at 25°C decreases with decreasing the temperature of the stock enzyme solution. The inactivation is completely reversible and is explained by cold‐induced dissociation of these hexameric enzymes into less active trimers.