The mechanism of action of primary alkylsulphohydrolase and arylsulphohydrolase from a detergent-degrading micro-organism

Cloves, J M; Dodgson, K. S.; Games, David E.; Shaw, Duncan; White, Graham F.

doi:10.1042/bj1670843

Cited by 30 publications

(16 citation statements)

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“…strain C12B, in which the constitutive and repressible P1 (2) and inducible P2 (7) are both present during growth on SDS. P1 and P2 have very similar chain-length substrate specificities but are clearly distinguishable by the mechanism of COOOS ester bond cleavage, i.e., OOS in P1 and COO in P2 (3,6). It will be interesting to determine in closer detail the substrate specificities and mechanisms of ester bond cleavage for the new enzymes AP1, AP2, AP3, and DP1; to this end, attempts are currently under way to purify and characterize DP1.…”

Section: Discussionmentioning

confidence: 99%

“…The P1 and P2 enzymes have been purified and characterized in detail. 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).…”

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confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

mentioning

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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“…Two possibilities then remained; either the mechanism is hydrolytic at the C-O bond or separation of SO~-occurs without the direct involvement of water molecules. Sulphatases acting on the C-O bond are a rarity confined to some long-chain alkylsulphatases (Bartholomew et al 1977;Shaw et al 1980;Cloves et al 1977). The majority of sulphatases so far examined hydrolyse at the O-S bond including all mammalian and microbial arylsulpharases (Dodgson et al 1982), choline sulphatase (Lucas et al 1972), D-lactate 2-sulphatase (Crescenzi et al 1984), 2,4-dichlorophenoxy ethylsulphatase (Lillis et al 1983) and butylsulphatase (unpublished observations).…”

Section: Incorporation Of ~So From H21somentioning

confidence: 99%

Oxygen-dependent desulphation of monomethyl sulphate by Agrobacterium sp. M3C

1990

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Agrobacterium sp. M3C, previously isolated from canal-water for its ability to grow on monomethyl sulphate, degraded this ester with stoichiometric liberation of inorganic sulphate. In contrast with the biodegradation of monomethyl sulphate in Hyphomicrobium sp., and of other longer-chain alkyl sulphates in Pseudomonas spp., the pathway in Agrobacterium appeared not to involve a sulphatase enzyme capable of catalysing ester-bond hydrolysis. No such sulphatase was detectable under a range of conditions of bacterial culture, or using various methods for preparing cell-extracts, or different assay conditions. There was no incorporation of 18O-label from H2(18O) into the liberated inorganic sulphate. No methanol was detectable during biodegradation, and the organism was incapable of growth on methanol, and did not produce methanol dehydrogenase activity when grown on monomethyl sulphate. Tracer studies using mono[14C]-methyl sulphate indicated that formate serine and glycine were produced during the biodegradation. The presence of these amino acids, together with high activity of hydroxypyruvate reductase, indicated the operation of the serine pathway common in methylotrophs. Use of an oxygen electrode in conjunction with monomethyl[35S]sulphate showed that release of 35SO2(-4) was dependent on availability of O2, and that there was equimolar stoichiometry among monomethyl sulphate degraded, O2 consumed and 35SO2(-4) released. A proposed pathway for the degradation involved an initial mono-oxygenation to methanediol monosulphate with subsequent elimination of SO2(-4) and concomitant formation of formaldehyde. The pathway was compared with degradation mechanisms for other C1 compounds and for other sulphate esters.

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“…With the symmetrical esters the question of inversion of configuration does not arise, but presumably here, too, C-O cleavage occurs. This mechanism is proving to be a common feature of both primary (Cloves et al, 1977) and secondary (Bartholomew et al, 1977) alkylsulphohydrolases in the detergent-degrading bacteria, Pseudomonas C 12B and C. terrigena, and contrasts sharply with the arylsulphohydrolases where, in all cases examined, S-0 cleavage is the rule (Spencer, 1958(Spencer, , 1959Cloves et al, 1977). Such divergence in behaviour must surely arise from fundamental differences in the mechanism of action of the two types of sulphohydrolase, although what these differences may be must, for the time, remain a mystery.…”

Section: Molecular-weight Determinationsmentioning

confidence: 99%

Substrate specificity and other properties of the inducible S3 secondary alkylsulphohydrolase purified from the detergent-degrading bacterium Pseudomonas C12B

Shaw¹,

Dodgson²,

White³

1980

Biochemical Journal

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The inducible S3 secondary alkylsulphohydrolase of the soil bacterium Pseudomonas C 12B was purified to homogeneity (683-fold from cell-free extracts by a combination of column chromatography on DEAE-cellulose, Sephadex G-100 and Blue Sepharose CL-6B. The enzyme has a molecular weight in the region of 40000-46 000, and is active over a broad range of pH from 5 to 9, with maximum activity at pH 8.2. The preferred substrates of the enzyme are the symmetrical secondary alkylsulphate esters such as heptan-4-yl sulphate and nonan-5-yl sulphate and the asymmetric secondary octyl and nonyl sulphate esters with the sulphate group attached to C-3 or C-4. However, for each asymmetric ester, the L-isomer is much more readily hydrolysed than the D-isomer. This specificity is interpreted in terms of a three-point attachment of the substrate to the enzyme's active site. The alkyl chains on either side of the esterified carbon atom are bound in two separate sites, one of which can only accommodate alkyl chains of limited size. The third site binds the sulphate group. Enzymic hydrolysis of this group is accompanied by complete inversion of configuration at the asymmetric carbon atom. The implied cleavage of the C-O bond of the C-O-S ester linkage was confirmed by 180-incorporation studies.

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The mechanism of action of primary alkylsulphohydrolase and arylsulphohydrolase from a detergent-degrading micro-organism

Cited by 30 publications

References 11 publications

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

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

Oxygen-dependent desulphation of monomethyl sulphate by Agrobacterium sp. M3C

Substrate specificity and other properties of the inducible S3 secondary alkylsulphohydrolase purified from the detergent-degrading bacterium Pseudomonas C12B

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