Arylsulfatase in Salmonella typhimurium: detection and influence of carbon source and tyramine on its synthesis.

AUTOR(ES)

Henderson, M J

RESUMO

Arylsulfatase synthesis was shown to occur in Salmonella typhimurium LT2. The enzyme had a molecular weight of approximately 50,000 and was separated into five forms by isoelectrofocusing. The optimal pH for substrate hydrolysis was pH 6.7, with Michaelis constants for nitrocatechol sulfate and nitrophenyl sulfate being 4.1 and 7.9 mM, respectively. Enzyme synthesis was strongly influenced by the presence of tyramine in the growth medium. The uptake of [14C]tyramine and arylsulfatase synthesis were initiated during the second phase of a diauxie growth response, when the organism was cultured with different carbon sources. Adenosine 3',5'-cyclic monophosphoric acid enhanced the uptake of tyramine and the levels of arylsulfatase synthesized. However, the addition of glucose and glycerol to organisms actively transporting tyramine and synthesizing enzyme caused a rapid inhibition of both of these processes. This inhibition was not reversed by adding adenosine 3',5'-cyclic monophosphoric acid. The results suggest that the effect of the carbon source on tyramine transport and arylsulfatase synthesis may be explained in terms of inducer exclusion.

Documentos Relacionados

• Regulation of derepressed synthesis of arylsulfatase by tyramine oxidase in Salmonella typhimurium.
• Tyramine oxidase and regulation of arylsulfatase synthesis in Klebsiella aerogenes.
• Derepression of Arylsulfatase Synthesis in Aerobacter aerogenes by Tyramine
• Mode of peptidoglycan synthesis in Salmonella typhimurium: single-strand insertion.
• Flagellar Synthesis in Salmonella typhimurium: Requirement for Ribonucleic Acid Synthesis1