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

Abstract

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'-cycic 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.

Sulfatases: Structure, Mechanism, Biological Activity, Inhibition, and Synthetic Utility

“…ARS activity has been identified in several species of enterobacteria ( Klebsiella ,63, 165 Salmonella ,166, 167 Proteus ,146, 168 Pseudomonas ,169 and Serrati 170), aquatic bacteria ( Alteromonas 52), pathogenic bacteria ( Mycobacteria 171, 172 and Pseudomonas 173, 174), extremophilic bacteria ( Plectonema 175), and soil bacteria ( Comamonas 176 and Pseudomonas 176). Indicative of their role in scavenging, most of the bacterial ARS enzymes are upregulated during sulfur starvation 3.…”

Riding the sulfur cycle – metabolism of sulfonates and sulfate esters in Gram-negative bacteria

“…Bacterial arylsulfatases have been identi¢ed and studied in a variety of species, including the enterobacteria (Klebsiella [98^100], Salmonella [101,102], Enterobacter [103,104], Proteus [105,106], Serratia [107]), pseudomonads (Pseudomonas [11,108,109], Comamonas [110]), mycobacteria, and cyanobacteria [111]. In recent years, however, genetic and biochemical studies have concentrated primarily on the arylsulfatase enzymes from Pseudomonas aeruginosa and Klebsiella pneumoniae, at least in part because these enzymes are closely related to the human arylsulfatases.…”

“…Two main conclusions can be drawn from the early biochemical studies: (i) most of the strains studied contained multiple arylsulfatase isozymes, and (ii) the arylsulfatase enzymes can be divided into two groups according to pH optimum, with one group showing optimal activity at pH values 6.5^7.1, and the other group at higher pH values of 8.3^9.0. Thus, Proteus rettgeri was reported to contain nine arylsulfatase isozymes, with pH optima at 6.7 and 8.3 [105,112], Serratia marcescens contains multiple isozymes with a broad pH optimum of 6.8^8.2 [107], P. aeruginosa has two isozymes with pH optima 9.0 and 8.4 [109,113], and Salmonella typhimurium has ¢ve enzymes, all with optimum pH 6.7 [102]. It should be noted, however, that multiple arylsulfatase bands have also been reported in two species (P. aeruginosa and K. pneumoniae) where later work revealed only one functional arylsulfatase gene.…”

Purification and Characterization of the Arylsulfatase Synthesized by Pseudomonas aeruginosa PAO During Growth in Sulfate‐Free Medium and Cloning of the Arylsulfatase Gene (atsA)

“…Salmonella typhimurium [41], Mycobacterium fortuitum [3] and Proteus rettgeri [42]. The two different sulfate-repressed arylsulfatases previously described in I?…”