Adenylate Cyclase from Brevibacterium liquefaciens. III. In Situ Regulation of Adenylate Cyclase by Pyruvate
AUTOR(ES)
Umezawa, Kazuo
RESUMO
In the presence of DL-alanine intracellular cyclic AMP in nonproliferating cells of Brevibacterium liquefaciens increased rapidly to the maximum level of approximately 180 μM, and extracellular cyclic AMP increased to 100 μM within 4 hr at 25°. Adenylate cyclase (EC 4.6.1.1) induction was not observed during this incubation. The concentration of pyruvate in the total culture increased concomitantly with that of cyclic AMP and reached approximately 20 mM after 4 hr of incubation. Since the activity of cyclic nucleotide phosphodiesterase is extremely low in this bacterium, the accumulation of cyclic AMP with DL-alanine appeared to be due to the activation of adenylate cyclase by pyruvate. D-alanine was more effective than L-alanine in producing pyruvate, and a high activity of D-alanine oxidation was detected in the cell lysate of B. liquefaciens.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=433935Documentos Relacionados
- Brevibacterium liquefaciens adenylate cyclase and its in vivo stimulation by pyruvate.
- Putative mediators of insulin action: regulation of pyruvate dehydrogenase and adenylate cyclase activities.
- OCCURRENCE OF NUCLEOTIDES IN CULTURE FLUIDS OF MICROORGANISMS III. : Nucleotide Excretion by Brevibacterium liquefaciens sp. n. with Special Reference to Uridine Diphospho-n-Acetylglucosamine Compounds
- Molar growth yields in Streptococcus faecalis var. liquefaciens.
- Regulation of adenylate cyclase in E. coli.