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- W2591639291 abstract "In the Claviceps strain SD58 the anthranilate synthetase was partially purified by fractionation with protamine sulfate and ammonium sulfate. The main activity (showing a 10–15 fold purification) was precipitated in the 30–50% (NH4)2SO4 fraction. The apparent Km values for the substrates chorismic acid, glutamine, NH4Cl and the cofactor Mg++ are ~ 0,04, ~ 4, ~ 8–9 and ~ 0,4 mM respectively. The pH-optima for the glutamine-dependent reaction are pH 7,8 and pH 8,6 respectively. A stimulatory effect of univalent cations on the ASSase was observed with increasing order by K+ > Na+, NH4+. The influence of bivalent ions was tested. Only Mn++- and Co++-ions can partially substitute the Mg++-ions. The enzyme was inhibited in the presence of tryptophane, chanoclavine, elymoclavine, indoleacrylic acid, prephenic acid and slightly activated in the presence of histidine. Histidine can not compensate the inhibition by tryptophan. The kinetic parameters of these inhibition- and activation reactions are described. In comparison to the strain SD58 the anthranilate synthetase from Claviceps purpurea, strain Pepty 695 (saprophytically alkaloids producing) and strain M5/95 F (saprophytically non-producing) was also studied. The properties of those enzymes are corresponding to the ASSase of the strain SD58." @default.
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- W2591639291 date "1976-01-01" @default.
- W2591639291 modified "2023-09-26" @default.
- W2591639291 title "Zur Charakterisierung der Anthranilat-Synthetase bei Claviceps" @default.
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- W2591639291 doi "https://doi.org/10.1016/s0015-3796(17)30897-1" @default.
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