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- W2034292122 abstract "Neocarratetraose 4-O-monosulphate β-hydrolase has been enriched 73-fold from the cell-free extract of Pseudomonas carrageenovora. This enzyme catalyses the hydrolysis of the β-glycosidic linkage of neocarratetraose 4-O-monosulphate [3,6-anhydro-α-d-galactopyranosyl-(1–>3)-1-d-galactopyranosyl-(1–>4)-3,6-anhydro-α-d-galactopyranosyl-(1–>3)- d-galactose 4-O-sulphate]. The products of hydrolysis are respectively neocarrabiose [3,6-anhydro-α-d-galactopyranosyl-(1–>3)- d-galactose] and neocarrabiose 4-O-sulphate [3,6-anhydro-α-d-galactopyranosyl-(1–>3)- d-galactose 4-O-sulphate]. During purification the χ-carrageenase and 4-sulphatase activities present in the bacterial extract were resolved from the title enzyme. From dodecylsalphate/polyacrylamide gel electrophoresis the enzyme has a molecular weight of 94000. Calcium stimulated the activity, Km 0.50 mmol dm−3. Optimal activity was found at pH 7.0 and the Km determined for the nominal substrate was 68 μmol dm−3. [14C]Neocarratetraose 4-O-monosulphate was prepared from [14C]carrageenan (Chondrus crispus) and utilized in a radiochemical assay for neocarratetraose 4-O-monosulphate β-hydrolase. Synthesis of [1-3H]neocarratetraitol 4-O-[35S]monosulphate yielded another substrate. This alditol was hydrolysed to yield a single radioactive species, thus supporting the position of sulphation of neocarratetraose 4-O-monosulphate deduced from 13C NMR studies. Neocarratetraose 4-O-disulphate [3,6-anhydro-α-d-galactopyranosyl-(1–>3)-4-O-sulphato-β-d-galactopyranosyl-(1–>4)-3,6-anhydro-α-d-galactopyranosyl-(1–>3)-d-galactose 4-O-sulphate] was not hydrolysed by the purified glycosidase. Tentative evidence for transglycosylation was obtained with both monosulphated substrates. A pathway is described for the sequential degradation of neocarratetraose 4-O-disulphate to neocarrabiose." @default.
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- W2034292122 date "1981-01-01" @default.
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- W2034292122 title "Neocarratetraose 4-O-Monosulphate beta-Hydrolase from Pseudomonas carrageenovora" @default.
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- W2034292122 doi "https://doi.org/10.1111/j.1432-1033.1981.tb05084.x" @default.
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