Solubilization and characterization of a SENECIONINE (cas 130-01-8) N-oxygenase from Crotalaria scassellatii seedlings
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Add time:09/30/2019 Source:infona.pl
Seeds of Crotalaria scassellatii (Fabaceae) store pyrrolizidine alkaloids as tertiary amines. During the beginning of seed germination the tertiary alkaloids are rapidly converted into the respective alkaloid N-oxides which are the ultimate forms of alkaloid transport, metabolism and storage in vegetative plant organs. The enzyme catalyzing the N-oxidation was isolated from 2-day old seedling, partially purified and characterized. It is a membrane-bound, but not microsomal enzyme sedimenting in the 39 000g fraction. The particulate enzyme was solubilized in the presence of 0.4% CHAPS and 0.4M NaCl. The solubilized enzyme was partially purified (228-fold) by means of 70% ammonium sulfate precipitation and monocrotaline affinity chromatography. Inhibitor experiments, temperature sensitivity and lack of a carboxy ferrocytochrome absorption maximum at 450nm strongly indicate SNO to be a flavin dependent enzyme. It is a mixed function monooxygenase that specifically N-oxidizes a number of structurally related pyrrolizidine alkaloids including the alkaloids of Crotalaria. A great variety of related alkaloids and xenobiotics were tested as substrates, none was accepted. The apparent K m values of SENECIONINE (cas 130-01-8), monocrotaline and heliotrine representing the three major types of pyrrolizidine alkaloids, are 12.4, 40.1 and 370.9μM, respectively. Senecionine is the best substrate, consequently the enzyme was named senecionine N-oxygenase (SNO). The substrate specificity of SNO is almost identical with that of a soluble insect SNO recently characterized from the haemolymph of arctiid larvae [Lindigkeit, R., Biller, A., Buch, M., Schiebel, H.-M., Boppré, M. and Hartmann, T., European Journal of Biochemistry, 1997, 245, 626].
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