Adenosine triphosphate and catabolite repression of β-galactosidase in escherichia coli

M. Aboud; M. Burger

doi:10.1016/0006-291X(71)90068-4

Adenosine triphosphate and catabolite repression of β-galactosidase in escherichia coli

M. Aboud, M. Burger

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

Addition of ATP to spheroplasts, induced for β-galactosidase synthesis, either in the presence of glycerol or in the absence of any carbon source, was found to reduce the differential rate of the enzyme formation. The effect of ADP, AMP, GTP, UTP and CTP was much weaker than that of ATP. Since the effect of ATP was reversed by cyclic AMP, it was concluded that ATP exerted its effect in the mechanism of catabolite repression.

Original language	English
Pages (from-to)	190-197
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	45
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(71)90068-4
State	Published - 1 Oct 1971
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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abstract = "Addition of ATP to spheroplasts, induced for β-galactosidase synthesis, either in the presence of glycerol or in the absence of any carbon source, was found to reduce the differential rate of the enzyme formation. The effect of ADP, AMP, GTP, UTP and CTP was much weaker than that of ATP. Since the effect of ATP was reversed by cyclic AMP, it was concluded that ATP exerted its effect in the mechanism of catabolite repression.",

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AB - Addition of ATP to spheroplasts, induced for β-galactosidase synthesis, either in the presence of glycerol or in the absence of any carbon source, was found to reduce the differential rate of the enzyme formation. The effect of ADP, AMP, GTP, UTP and CTP was much weaker than that of ATP. Since the effect of ATP was reversed by cyclic AMP, it was concluded that ATP exerted its effect in the mechanism of catabolite repression.

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Adenosine triphosphate and catabolite repression of β-galactosidase in escherichia coli

Abstract

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