Regulation of derepressed synthesis of arylsulfatase by tyramine oxidase in Salmonella typhimurium

Murooka, Y; Harada, Tokuya

doi:10.1128/jb.145.2.796-802.1981

Cited by 24 publications

(13 citation statements)

References 18 publications

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“…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.…”

Section: Substrates and Biological Functions Of Prokaryotic Sulfatmentioning

confidence: 99%

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

2004

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Sulfatases, which cleave sulfate esters in biological systems, play a key role in regulating the sulfation states that determine the function of many physiological molecules. Sulfatase substrates range from small cytosolic steroids, such as estrogen sulfate, to complex cell-surface carbohydrates, such as the glycosaminoglycans. The transformation of these molecules has been linked with important cellular functions, including hormone regulation, cellular degradation, and modulation of signaling pathways. Sulfatases have also been implicated in the onset of various pathophysiological conditions, including hormone-dependent cancers, lysosomal storage disorders, developmental abnormalities, and bacterial pathogenesis. These findings have increased interest in sulfatases and in targeting them for therapeutic endeavors. Although numerous sulfatases have been identified, the wide scope of their biological activity is only beginning to emerge. Herein, accounts of the diversity and growing biological relevance of sulfatases are provided along with an overview of the current understanding of sulfatase structure, mechanism, and inhibition.

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Section: Substrates and Biological Functions Of Prokaryotic Sulfatmentioning

confidence: 99%

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

2004

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“…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.…”

Section: Bacterial Arylsulfatasesmentioning

confidence: 99%

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

2000

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Sulfonates and sulfate esters are widespread in nature, and make up over 95% of the sulfur content of most aerobic soils. Many microorganisms can use sulfonates and sulfate esters as a source of sulfur for growth, even when they are unable to metabolize the carbon skeleton of the compounds. In these organisms, expression of sulfatases and sulfonatases is repressed in the presence of sulfate, in a process mediated by the LysR-type regulator protein CysB, and the corresponding genes therefore constitute an extension of the cys regulon. Additional regulator proteins required for sulfonate desulfonation have been identified in Escherichia coli (the Cbl protein) and Pseudomonas putida (the AsfR protein). Desulfonation of aromatic and aliphatic sulfonates as sulfur sources by aerobic bacteria is oxygendependent, carried out by the K-ketoglutarate-dependent taurine dioxygenase, or by one of several FMNH 2 -dependent monooxygenases. Desulfurization of condensed thiophenes is also FMNH 2 -dependent, both in the rhodococci and in two Gram-negative species. Bacterial utilization of aromatic sulfate esters is catalyzed by arylsulfatases, most of which are related to human lysosomal sulfatases and contain an active-site formylglycine group that is generated post-translationally. Sulfate-regulated alkylsulfatases, by contrast, are less well characterized. Our increasing knowledge of the sulfur-regulated metabolism of organosulfur compounds suggests applications in practical fields such as biodesulfurization, bioremediation, and optimization of crop sulfur nutrition. ß

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“…33) In E. coli cells that carried the plasmid containing the alsA, the synthesis of arylsulfatase was repressed by various sources of sulfur including methionine and taurine. Methionine and taurine caused to repression of the enzyme synthesis in K. aerogene.\• but strongly repressed it in S. fyphimllrillm 34 ) and S. marcescells. 18 ) These organism-specific differences in the degree of the repression may be due to differences in the metabolic conversion of methionine or taurine into the actual corepressor for the atsR gene.…”

Section: Cloning and Characterization Of At!! Operonmentioning

confidence: 93%

The Monoamine Regulon Including Syntheses of Arylsulfatase and Monoamine Oxidase in Bacteria

Murooka

Azakami

Yamashita

1996

Bioscience, Biotechnology, and Biochemistry

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Bacterial cells respond to monoamine compounds, such as tyramine, dopamine, octopamine, or norepinephrine, and induce the syntheses of tyramine oxidase encoded by tynA and monoamine oxidase encoded by maoA. These monoamine compounds also derepress the synthesis of atsA-specified arylsulfatase that is repressed by sulfur compounds. These complex mechanisms of regulons regulated by monoamine and sulfur compounds has been analyzed by cloning and characterization of genes that are involved in the repression and derepression of the synthesis of arylsulfatase. The atsA gene forms an operon with the atsB gene, which encodes an activator of the expression of atsA. The negative regulator gene for arylsulfatase was found to code for dihydrofolate reductase (folA). The maoA gene forms an operon with the maoC gene, which has similarity to a dehydrogenase involved in the tyramine metabolism. The moaF gene encoding a 30-kDa protein, which is induced by tyramine, also forms an operon with the moaE gene. Finally, the moaR gene, which is induced by monoamine, was found to play a central role in the positive regulation of the expression of the monoamine regulon (moa) including the atsBA, maoCA, moaEF, and tyn operons. The moaR expression is subject to autogenous regulation and to cAMP-CRP control. The MoaR protein has a helix-turn-helix motif in its C terminus. Thus, the MoaR protein probably regulates the operons by binding to the regulatory region of the moa regulon.

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Regulation of derepressed synthesis of arylsulfatase by tyramine oxidase in Salmonella typhimurium

Cited by 24 publications

References 18 publications

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

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

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

The Monoamine Regulon Including Syntheses of Arylsulfatase and Monoamine Oxidase in Bacteria

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