Evidence Against the Presence of 3′, 5′-Cyclic Adenosine Monophosphate and Relevant Enzymes in Lactobacillus plantarum

AUTOR(ES)

Sahyoun, N.

RESUMO

Analysis of cells of Lactobacillus plantarum, starved or undergoing induction, showed no 3′, 5′-cyclic adenosine monophosphate (cAMP). Neither adenyl cyclase nor 3′, 5′-cAMP phosphodiesterase was detected in extracts. Extracts of L. plantarum did not inhibit these two enzymes of Escherichia coli K-12, strain W1435. Incubation of adenosine triphosphate (ATP)-U-14C with cells or various cell-free fractions of L. plantarum did not produce labeled 3′, 5′-cAMP. Of various 3′, 5′-cyclic and acyclic nucleotides tested, only 3′, 5′-cAMP, ATP, and yeast adenylic acid stimulated l-arabinose isomerase. Yeast adenylic acid was two to four times as effective as 3′, 5′-cAMP or ATP. 2′, 3′-cAMP was not effective.

Documentos Relacionados

• Control of Neurospora crassa morphology by cyclic adenosine 3', 5'-monophosphate and dibutyryl cyclic adenosine 3', 5'-monophosphate.
• The content and metabolism of cyclic adenosine 3', 5'-monophosphate and cyclic guanosine 3', 5'-monophosphate in adenocarcinoma of the human colon.
• Control and localization of rat adrenal cyclic guanosine 3', 5'-monophosphate. Comparison with adrenal cyclic adenosine 3', 5'-monophosphate.
• Cyclic 3', 5'-adenosine monophosphate phosphodiesterase mutants of Salmonella typhimurium.
• Requirement of Adenosine 3′, 5′-Cyclic Phosphate for Flagella Formation in Escherichia coli and Salmonella typhimurium