The epimerization of ecdysone to 3-epiecdysone has been investigated in a dialysed cytosolic enzyme preparation from midgut of sixth instar Spodoptera littoralis larvae, with particular emphasis on establishing the intermediacy of 3-dehydroecdysone. Incubation of ecdysone with the dialysed cytosolic preparation furnished 3-dehydroecdysone as the only detectable product, the reaction being oxygen-dependent. The enzyme preparation catalysed reduction of 3-dehydroecdysone to 3-epiecdysone and ecdysone in the presence of NADH or NADPH. Whereas formation of 3-epiecdysone greatly predominated over that of ecdysone in the presence of NADPH, the converse applied when the cofactor was NADH. 3-Epiecdysone incubated with the enzyme preparation in the presence of various cofactors was not metabolized, indicating the irreversibility of the reduction of 3-dehydroecdysone to 3-epiecdysone and, hence, of the 3-epimerization process. The foregoing results, together with comparison of the metabolism of 3-dehydro[3H]ecdysone and [3H]ecdysone by the enzyme preparation in the presence of unlabelled ecdysone and NADPH, support the intermediacy of 3-dehydroecdysone in the 3-epimerization of ecdysone.
Research Article|October 15 1985
Involvement of 3-dehydroecdysone in the 3-epimerization of ecdysone
Biochem J (1985) 231 (2): 369-374.
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N P Milner, H H Rees; Involvement of 3-dehydroecdysone in the 3-epimerization of ecdysone. Biochem J 15 October 1985; 231 (2): 369–374. doi: https://doi.org/10.1042/bj2310369
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