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FEBS Lett. 1995 Feb 6;359(1):20-2.

Cold lability of the mutant forms of Escherichia coli inorganic pyrophosphatase.

Author information

1
A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.

Erratum in

  • FEBS Lett 1995 Apr 10;362(3):347.

Abstract

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 degrees C: their activity measured at 25 degrees 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.

PMID:
7851523
DOI:
10.1016/0014-5793(95)00003-r
[Indexed for MEDLINE]
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