Glycosulfatase of Pseudomonas Carrageenovora: Desulfation of Disaccharide From Κ- Carrageenan

Weigl, Josef; Yaphe, W.

doi:10.1139/m66-118

Cited by 24 publications

(22 citation statements)

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“…Side reactions such as desulfatation of organic compounds (Weigl & Yaphe 1966, Fitzgerald 1976 were also affected by relatively high temperature optima (45°C) of sulfatase in Antarctic sediments, although 60°C temperature optima have been reported for sediments from lower latitudes (Oshrain & Wiebe 1979). A considerably lower optimum (30°C) characterized alkaline phosphatase from the same source (Fig.…”

Section: Discussionmentioning

confidence: 99%

Differential temperature effects on the efficiency of carbon pathways in Antarctic marine benthos

Reichardt¹

1987

Mar. Ecol. Prog. Ser.

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Enzymatic activ~ties and metabolic rates, which play key roles in benthic carbon turnover. were character~zed w~t h respect to cold adaptation In aphotic Antarctic sediments. Temperature optima for CO2 dark fixation and mineralization of glucose coincided largely \nth the maximal growth temperatures of obligate psychrophilic bacteria (at 20°C and below). On the other hand, predominantly extracellular enzyme activities involved in the conversion of particulate organic matter (POM) into dissolved organic matter [DOIVI), such as scleroprotease and chitinase, had considerably higher temperature ophma (40 to 55°C) This lack of cold adaptation at the activity level was less strongly expressed in other hydrolases [sulfatase, alkaline phosphatase). Substrate affinihes or a c t~v a t~o n energles were often inapplicable or insignificant as a potential measure of temperature adaptation. Alternative strategies of cold adaptation may be relevant at the level of synthesis of POM-solubilizing enzymes.

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Section: Discussionmentioning

confidence: 99%

Differential temperature effects on the efficiency of carbon pathways in Antarctic marine benthos

Reichardt¹

1987

Mar. Ecol. Prog. Ser.

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“…The pioneering work of Weigl and Yaphe (1966) demonstrated the first carrageenan sulfatase activity in protein extracts prepared from the marine bacterium P. carrageenovora. Ten years later, this enzyme-a 4O-κ-carrabiose sulfatase of about 55 kDawas purified and NMR revealed an exo-type mode of action.…”

Section: Biochemically Characterized Marine Polysaccharide Sulfatasesmentioning

confidence: 99%

Marine Polysaccharide Sulfatases

Helbert

2017

Front. Mar. Sci.

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Polysaccharides are the most abundant and the most complex organic molecules in the ocean. In contrast to land polysaccharides, many marine polysaccharides are highly sulfated; in particular, the cell walls of macroalgae harbor a high diversity of sulfated polysaccharides (carrageenans, agarans, fucoidans, ulvans, etc.). These sulfated polysaccharides, biosynthesized by macroalgal primary producers, represent an important food source for heterotrophic organisms. Their biodegradation requires a set of enzymes that can cleave the glycosidic linkages of the carbohydrate backbone (called glycoside hydrolases) and the sulfate ester groups (called polysaccharide sulfatases). This review first provides on overview of the current state of knowledge on the classification and mechanisms of sulfatases in general. Then, based on an exploration of marine genomic and metagenomics data that reveals the diversity of carbohydrate sulfatases, it focuses on strategies to predict these sulfatases. In particular, the modularity of sulfatases and their location in marine polysaccharide utilization loci (PUL) provide clues as to their potential substrates and can drive future functional assays. Finally, the review underscores the low number of currently biochemically characterized marine carbohydrate sulfatases (e.g., agarases, carrageenanases, and fucose sulfatases). Bottlenecks encountered in studies on sulfatases likely lie in the difficulties in purifying them and producing them in heterologous systems.

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“…Two substrates have been investigated, namely neocarrabiose 4-0-sulphate and neocarratetraose 4-0-sulphate, the two simplest degradation products of x-carrageenase digestion of x-carrageenan. In a previous study of this enzyme by Weigl and Yaphe [5], neocarrabiose 4-0-sulphate as well as galactose 4-0-sulphate and galactose 6-0-sulphate were tested as potential substrates for a partially purified glycosulphatase. These authors reported activity with neocarrabiose 4-0-sulphate and galactose 6-0-sulphate but not with galactose 4-0-sulphate.…”

Section: Action Of Purfied Glycosulphatase On [ 35 S]oligosaccharidesmentioning

confidence: 99%

Glycosulphatase from Pseudomonas carrageenovora. Purification and Some Properties

McLEAN

Williamson

1979

Eur J Biochem

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A glycosulphatase present in the soluble fraction of disrupted Pseudomonas carrageenovora has been purified 500-fold by gel filtration on Sephacryl S-200 and ion-exchange chromatography on DEAE-Sepharose CL-6B. By dodecylsulphate/polyacrylamide gel electrophoresis the enzyme is practically homogeneous and has a molecular weight of 55 000. Conditions of optimal sodium chloride concentration and pH at 25 "C were 0.25-0.50 mol dm-3 and pH 7.0 respectively. The purified enzyme was inhibited by inorganic phosphate.Preparation is described of neocarrabiose 4-0-[35S]sulphate and neocarratetraose 4-0-[35S]-sulphate from labelled Chondrus crispus. The purified glycosulphatase is active against both these substrates although only one of the two sulphate esters in the tetrasaccharide is hydrolysed. Analysis of the reaction products was by gel filtration, electrophoresis and I3C nuclear magnetic resonance spectroscopy. The results are consistent with the products of desulphation being respectively neocarrabiose and neocarratetraose 4-0-monosulphate with the sulphate ester proximal to the reducing end [ 3,6-anhydro-a-~-galactopyranosyl-(Sulphatases have been detected ubiquitously in organisms [l -31 pertinent examples being bacteria [4,5] and algae [6,7]. In the degradation of chondroitin sulphate by Proteus vulgaris [4] only disaccharide oligomers are susceptible to the relevant sulphatases. This contrasts with the algal sulphatases [6,7], which release sulphate at the polymer level from galactose 6-0-sulphate residues with concomitant formation of the 3,6-anhydro derivative.In the initial description of a glycosulphatase from Pseudomonas carrageenovora by Weigl and Yaphe [5], the partially purified enzyme was tested with several sugar sulphates. We consider this enzyme to be potentially applicable in the study of carrageenan fragments, and present a satisfactory purification method.Preparation of neocarratetraose 4-0-[35S]sulphate and neocarratetraose 4-0-[35S]sulphate of high radiochemical purity allowed the development of a practical assay similar to that described for choline sulphatase [8]. These oligosaccharides were isolated after x-carrageenase digestion of [35S]carrageenan extracted from Chondrus crispus cultured in the presence of inorganic [35S]sulphate.

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Glycosulfatase of Pseudomonas Carrageenovora: Desulfation of Disaccharide From Κ- Carrageenan

Cited by 24 publications

References 0 publications

Differential temperature effects on the efficiency of carbon pathways in Antarctic marine benthos

Differential temperature effects on the efficiency of carbon pathways in Antarctic marine benthos

Marine Polysaccharide Sulfatases

Glycosulphatase from Pseudomonas carrageenovora. Purification and Some Properties

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