Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea

Robert J. Grebenok; David W. Galbraith; Irene Benveniste; Rene Feyereisen

doi:10.1016/0031-9422(96)00094-5

Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea

Robert J. Grebenok, David W. Galbraith, Irene Benveniste, Rene Feyereisen

Research output: Contribution to journal › Article › peer-review

21 Scopus citations

Abstract

A microsomal preparation isolated from first leaves of 25-day-old spinach catalysed the hydroxylation of ecdysone to produce the insect moulting hormone, 20-hydroxyecdysone. Hydroxylation was dependent on NADPH and molecular oxygen, and was inhibited by carbon monoxide. Carbon monoxide inhibition was partially reversible by white light. Polyclonal antibodies to the Jerusalem artichoke NADPH-cytochrome P450 reductase inhibited the hydroxylation reaction as well as the spinach microsomal NADPH cytochrome c reductase. These results taken together establish ecdysone hydroxylation as a cytochrome P450 dependent reaction in spinach, which is known to synthesize large amounts of phytoecdysteroids.

Original language	English (US)
Pages (from-to)	927-933
Number of pages	7
Journal	Phytochemistry
Volume	42
Issue number	4
DOIs	https://doi.org/10.1016/0031-9422(96)00094-5
State	Published - Jul 1996

Keywords

20-hydroxyecdysone
Chenopodiaceae
Spinacia oleracea
cytochrome P450
ecdysone
enzymology
monooxygenase
oleracea
phytoecdysteroids

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Plant Science
Horticulture

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10.1016/0031-9422(96)00094-5

Cite this

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title = "Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea",

abstract = "A microsomal preparation isolated from first leaves of 25-day-old spinach catalysed the hydroxylation of ecdysone to produce the insect moulting hormone, 20-hydroxyecdysone. Hydroxylation was dependent on NADPH and molecular oxygen, and was inhibited by carbon monoxide. Carbon monoxide inhibition was partially reversible by white light. Polyclonal antibodies to the Jerusalem artichoke NADPH-cytochrome P450 reductase inhibited the hydroxylation reaction as well as the spinach microsomal NADPH cytochrome c reductase. These results taken together establish ecdysone hydroxylation as a cytochrome P450 dependent reaction in spinach, which is known to synthesize large amounts of phytoecdysteroids.",

keywords = "20-hydroxyecdysone, Chenopodiaceae, Spinacia oleracea, cytochrome P450, ecdysone, enzymology, monooxygenase, oleracea, phytoecdysteroids",

author = "Grebenok, {Robert J.} and Galbraith, {David W.} and Irene Benveniste and Rene Feyereisen",

year = "1996",

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journal = "Phytochemistry",

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T1 - Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea

AU - Grebenok, Robert J.

AU - Galbraith, David W.

AU - Benveniste, Irene

AU - Feyereisen, Rene

PY - 1996/7

Y1 - 1996/7

N2 - A microsomal preparation isolated from first leaves of 25-day-old spinach catalysed the hydroxylation of ecdysone to produce the insect moulting hormone, 20-hydroxyecdysone. Hydroxylation was dependent on NADPH and molecular oxygen, and was inhibited by carbon monoxide. Carbon monoxide inhibition was partially reversible by white light. Polyclonal antibodies to the Jerusalem artichoke NADPH-cytochrome P450 reductase inhibited the hydroxylation reaction as well as the spinach microsomal NADPH cytochrome c reductase. These results taken together establish ecdysone hydroxylation as a cytochrome P450 dependent reaction in spinach, which is known to synthesize large amounts of phytoecdysteroids.

AB - A microsomal preparation isolated from first leaves of 25-day-old spinach catalysed the hydroxylation of ecdysone to produce the insect moulting hormone, 20-hydroxyecdysone. Hydroxylation was dependent on NADPH and molecular oxygen, and was inhibited by carbon monoxide. Carbon monoxide inhibition was partially reversible by white light. Polyclonal antibodies to the Jerusalem artichoke NADPH-cytochrome P450 reductase inhibited the hydroxylation reaction as well as the spinach microsomal NADPH cytochrome c reductase. These results taken together establish ecdysone hydroxylation as a cytochrome P450 dependent reaction in spinach, which is known to synthesize large amounts of phytoecdysteroids.

KW - 20-hydroxyecdysone

KW - Chenopodiaceae

KW - Spinacia oleracea

KW - cytochrome P450

KW - ecdysone

KW - enzymology

KW - monooxygenase

KW - oleracea

KW - phytoecdysteroids

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VL - 42

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ER -

Ecdysone 20-monooxygenase, a cytochrome P450 enzyme from spinach, Spinacia oleracea

Abstract

Keywords

ASJC Scopus subject areas

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