Sulfur Metabolism of Aerobacter aerogenes. I. A Repressible Sulfatase

Rammler, D. H.; Grado, Carmen; Fowler, L.R.

doi:10.1021/bi00890a014

Cited by 58 publications

(49 citation statements)

References 11 publications

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“…In both soil bacteria, such as Psetrdomonas strain C12B (George & Fitzgerald,l98l), and enteric bacteria, such as Klebsiella aerogenes (Rammler et al, 1964;Adachi e t al., 1975;Murookaetal., 1978;Okaetal., 1980) andsalmonella typbimtrritlm (Henderson & Milazzo, 1979), as well as in Abbreviations: ASW, artificial sea water; HCA, hydrophobic cluster analysis; IEF, isoelectric focalization; MUF, 4-methylumbelliferone; MUF-S, 4-methylumbelliferyl sulphate.…”

Section: Introductionmentioning

confidence: 99%

Arylsulphatase from Alteromonas carrageenovora

et al. 1995

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Arylsulphatase activity was identified in cultures of the marine bacterium Alteromonas carrageenovora, using methylumbelliferyl sulphate as substrate. In contrast with most other microbial arylsulphatases, arylsulphatase production in A. carrageenovora was not repressed by sulphate. The structural gene of arylsulphatase (atsA) was cloned and sequenced. An ORF of 984 bp was found, specifying a primary translation product of 328 amino acids with a molecular mass of 35797 Da. Arylsulphatase was partially purified from cell extracts of both A. carrageenovora and recombinant Escherichia coli. Both the recombinant and native enzymes exhibited a pl of 55, a Michaelis constant for methylumbelliferyl sulphate of 68 pM, and a molecular mass of approximately 35000 Da in SDS-PAGE analysis. Secondary structure comparisons using hydrophobic cluster analysis suggest functional analogies between the arylsulphatase of A. carrageenovora, #at of Mycobacterium leprae and a 33.5 kDa protein from Porphymmonas gingivalis. It is speculated that these proteins are all glycosulphohydrolases, involved with desulphatation of sul pha ted pol ysaccha rides.

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Section: Introductionmentioning

confidence: 99%

Arylsulphatase from Alteromonas carrageenovora

et al. 1995

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“…While they have the same exclusive specificity for LPAS, they are distinguishable on the basis of the mechanism of COOOS ester bond cleavage (OOS and COO for P1 and P2, respectively) and the regulation of synthesis (P1 is constitutive and P2 is inducible) (2,6,7). Alkylsulfatase activity has also been found in Pseudomonas aeruginosa (11) and Aerobacter aerogenes (24). Comamonas terrigena produces two secondary alkylsulfatases (CS1 and CS2) active on various secondary alkyl sulfates (19).…”

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confidence: 99%

Novel Alkylsulfatases Required for Biodegradation of the Branched Primary Alkyl Sulfate Surfactant 2-Butyloctyl Sulfate

Ellis

Hales

Ur-Rehman

et al. 2002

Appl Environ Microbiol

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Recent reports show that contrary to common perception, branched alkyl sulfate surfactants are readily biodegradable in standard biodegradability tests. We report here the isolation of bacteria capable of biodegrading 2-butyloctyl sulfate and the identification of novel enzymes that initiate the process. Enrichment culturing from activated sewage sludge yielded several strains capable of growth on 2-butyloctyl sulfate. Of these, two were selected for further study and identified as members of the genus Pseudomonas. Strain AE-A was able to utilize either sodium dodecyl sulfate (SDS) or 2-butyloctyl sulfate as a carbon and energy source for growth, but strain AE-D utilized only the latter. Depending on growth conditions, strain AE-A produced up to three alkylsulfatases, as shown by polyacrylamide gel electrophoresis zymography. Growth on either SDS or 2-butyloctyl sulfate or in nutrient broth produced an apparently constitutive, nonspecific primary alkylsulfatase, AP1, weakly active on SDS and on 2-butyloctyl sulfate. Growth on 2-butyloctyl sulfate produced a second enzyme, AP2, active on 2-butyloctyl sulfate but not on SDS, and growth on SDS produced a third enzyme, AP3, active on SDS but not on 2-butyloctyl sulfate. In contrast, strain AE-D, when grown on 2-butyloctyl sulfate (no growth on SDS), produced a single enzyme, DP1, active on 2-butyloctyl sulfate but not on SDS. DP1 was not produced in broth cultures. DP1 was induced when residual 2-butyloctyl sulfate was present in the growth medium, but the enzyme disappeared when the substrate was exhausted. Gas chromatographic analysis of products of incubating 2-butyloctyl sulfate with DP1 in gels revealed the formation of 2-butyloctanol, showing the enzyme to be a true sulfatase. In contrast, Pseudomonas sp. strain C12B, well known for its ability to degrade linear SDS, was unable to grow on 2-butyloctyl sulfate, and its alkylsulfatases responsible for initiating the degradation of SDS by releasing the parent alcohol exhibited no hydrolytic activity on 2-butyloctyl sulfate. DP1 and the analogous AP2 are thus new alkylsulfatase enzymes with novel specificity toward 2-butyloctyl sulfate.Synthetic surfactants are components of a variety of household and industrial detergent formulations. Other industrial applications include paints, textiles and fabrics, oil-spill dispersants, concrete, paper, lubricants, and many others (14,15,26). In 1990, world production of synthetic surfactants was 7 megatonnes (Mt) per annum, of which 5.3 Mt came from the United States, the European Union, and Japan (12). Of this part, 1.74 Mt per annum was anionic surfactant, a significant quantity which reflects the high demand for this type of surfactant. The anionic surfactant group embraces a range of compounds distinguished on the basis of chemical structure and includes primary alkyl sulfates, such as sodium dodecyl sulfate (SDS), and linear secondary alkyl sulfates, such as dodecyl 2-sulfate. Synthetic primary alkyl sulfates are based on feedstocks derived from long-chain olefins by us...

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“…Unlike the alkylsulfatases, most of the arylsulfatases are not synthesized constitutively, but are subject to strict sulfur derepression control. They have been studied in various pseudomonads [101], in Klebsiella aerogenes [112][113][114], Serratia marcescens [ 115], Salmonella typhimurium [ 116], Enterobacter aerogenes [117,118], and in Proteus rettgeri [119]. These enzymes are also present in fungi (reviewed in [101]) and in higher organisms.…”

Section: Arylsulfatesmentioning

confidence: 99%

Microbial metabolism of sulfurand phosphorus-containing xenobiotics

Kertesz

1994

FEMS Microbiology Reviews

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Abstract:The enzymes involved in the microbial metabolism of many important phosphorus-or sulfur-containing xenobiotics, including organophosphate insecticides and precursors to organosulfate and organosulfonate detergents and dyestuffs have been characterized. In several instances their genes have been cloned and analysed. For phosphonate xenobiotics, the enzyme system responsible for the cleavage of the carbon-phosphorus bond has not yet been observed in vilro, though much is understood on a genetic level about phosphonate degradation. Phosphonate metabolism is regulated as part of the Pho regulon, under phosphate starvation control. For organophosphorothionate pesticides the situation is not so clear, and the mode of regulation appears to depend on whether the compounds are utilized to provide phosphorus, carbon or sulfur for cell growth. The same is true for organosulfonate metabolism, where different (and differently regulated) enzymatic pathways are involved in the utilization of sulfonates as carbon and as sulfur sources, respectively. Observations at the protein level in a number of bacteria suggest that a regulatory system is present which responds to sulfate limitation and controls the synthesis of proteins involved in providing sulfur to the cell and which may reveal analogies between the regulation of phosphorus and sulfur metabolism.

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Sulfur Metabolism of Aerobacter aerogenes. I. A Repressible Sulfatase

Cited by 58 publications

References 11 publications

Arylsulphatase from Alteromonas carrageenovora

Arylsulphatase from Alteromonas carrageenovora

Novel Alkylsulfatases Required for Biodegradation of the Branched Primary Alkyl Sulfate Surfactant 2-Butyloctyl Sulfate

Microbial metabolism of sulfurand phosphorus-containing xenobiotics

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