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Ecdysone 20-monooxygenase

ecdysone 20-monooxygenase
Identifiers
EC no.1.14.99.22
CAS no.55071-97-1
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Ecdysone 20-monooxygenase (EC 1.14.99.22) is an enzyme that catalyzes the chemical reaction

ecdysone + AH2 + O2 20-hydroxyecdysone + A + H2O

The three substrates of this enzyme are ecdysone, an electron acceptor AH2, and O2, whereas its three products are 20-hydroxyecdysone, the reduction product A, and H2O.[1][2][3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derive from O miscellaneous. The systematic name of this enzyme class is ecdysone,hydrogen-donor:oxygen oxidoreductase (20-hydroxylating). Like other genes in the ecdysone synthesis pathway, it belongs to Cytochrome P450 Halloween genes, with the nickname shade, other names in common use include alpha-ecdysone C-20 hydroxylase, and ecdysone 20-hydroxylase.[4]

References

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  1. ^ Johnson P, Rees HH (1977). "The mechanism of C-20 hydroxylation of alpha-ecdysone in the desert locust, Schistocerca gregaria". Biochemical Journal. 168 (3): 513–520. doi:10.1042/bj1680513. PMC 1183799. PMID 606249.
  2. ^ Nigg HN, Svoboda JA, Thompson MJ, Dutky SR, Kaplanis JN, Robbins WE (1976). "Ecdysome 20-hydroxylase from the midgut of the tobacco hornworm (Manduca sexta L.)". Experientia. 32 (4): 438–439. doi:10.1007/BF01920781. PMID 5286. S2CID 8962617.
  3. ^ Gilbert LI; Bollenbacher, WE; Cooper, DY; Schleyer, H; Wielgus, JJ; Gilbert, LI (1979). "Ecdysone 20-monooxygenase: characterization of an insect cytochrome p-450 dependent steroid hydroxylase". Molecular and Cellular Endocrinology. 15 (3): 111–133. doi:10.1016/0303-7207(79)90033-9. PMID 488526. S2CID 25731761.
  4. ^ Petryk A, Warren JT, Marques G, Jarcho MP, Gilbert LI, Kahler J, Parvy JP, Li YT, Dauphin-Villemant C, O'Connor MB (2003). "Shade is the Drosophila P450 enzyme that mediates the hydroxylation of ecdysone to the steroid insect molting hormone 20-hydroxyecdysone". Proceedings of the National Academy of Sciences of the United States of America. 100 (24): 13773–13778. doi:10.1073/pnas.2336088100. PMC 283497. PMID 14610274.