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- W2017009902 abstract "Tigloyl-CoA:pseudotropine acyl transferase esterifies the 3β-hydroxyl group of pseudotropine (3β-hydroxytropane) with the tiglic acid moiety of tigloyl-Coenzyme A. This enzyme was purified to near electrophoretic homogeneity—about 330-fold—from transformed root cultures of Datura stramonium. The protocol involved the sequential use of ammonium sulphate precipitation, hydrophobic interaction, anion-exchange, chromatofocusing and gel filtration chromatography. The enzyme has a Mr of 65 000, as determined by gel filtration chromatography on Sepharose 6 and SDS-PAGE electrophoresis, indicating it to be active as a monomer. Maximal activity occurs at pH 9.0 but the enzyme is still about 30% active at pH 7.0. The purified protein shows simple Michaelis-Menten kinetic behaviour, with Km values of 0.36 and 1.31 mM for pseudotropine and tigloyl-CoA, respectively. The enzyme is specific for the acyl group receptor. Of a range of potential acceptors tested, only pseudotropine and 4-hydroxy-1-methylpiperidine (14%) were used: tropine (3α-hydroxytropane) and norpseudotropine were not acylated. In contrast, the enzyme possesses the ability to transfer the acyl moiety to pseudotropine from a wide range of aliphatic acyl-CoA thioesters. Tigloyl-CoA and acetyl-CoA act recuprocally as competitive inhibitors, suggesting that they compete for the same active site on the enzyme. With acetyl-CoA the Km is 0.33 mM, indicating that the enzyme has a higher affinity for this acyl donor than for tigloyl-CoA. Neither CoA nor any of the alkamine acceptors tested were able to inhibit the acylation of pseudotropine." @default.
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- W2017009902 title "Tigloyl-CoA:pseudotropine acyl transferase—An enzyme of tropane alkaloid biosynthesis" @default.
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- W2017009902 doi "https://doi.org/10.1016/0031-9422(94)00907-b" @default.
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