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Regulation of Maltodextrin Phosphorylase Synthesis in Escherichia coli by Cyclic Adenosine 3', 5'-Monophosphate and Glucose¹

^a Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50010

ABSTRACT

Cyclic adenosine 3', 5'-monophosphate (AMP) stimulates maltodextrin phosphorylase synthesis in Escherichia coli cells induced with maltose. A maximal effect occurs at 2 to 3 mM cyclic AMP. The action of cyclic AMP is specific, inasmuch as adenosine triphosphate, 3'-AMP, 5'-AMP, adenosine, and dibutyryl cyclic AMP are inactive. Glucose, -methyl glucoside, 2-deoxyglucose, and pyridoxal 5'-phosphate repress maltodextrin phosphorylase synthesis. This repression is reversed by cyclic AMP. The action of cyclic AMP appears to be at the transcriptional level, since cyclic AMP fails to stimulate phosphorylase production in induced cells in which messenger ribonucleic acid synthesis has been arrested by rifampin or by inducer removal. The two other enzymes involved in the metabolism of maltose, amylomaltase and maltose permease, are also induced in this strain of E. coli and affected by glucose and cyclic AMP in a manner similar to phosphorylase.

² Present address: The Biological Sciences Group, The University of Connecticut, Storrs, Conn. 06268.

³ Present Address: Biochemistry Department, The University of Iowa, Iowa City, Iowa 52240.

¹ Journal paper J-7119 (project no. 1843) of the Iowa Agriculture and Home Economics Experiment Station, Ames, Iowa.