Cold lability of the mutant forms of Escherichia coli inorganic pyrophosphatase.
FEBS Lett
; 359(1): 20-2, 1995 Feb 06.
Article
en En
| MEDLINE
| ID: mdl-7851523
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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Pirofosfatasas
/
Frío
/
Escherichia coli
Idioma:
En
Revista:
FEBS Lett
Año:
1995
Tipo del documento:
Article