(2002) A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.
My colleagues and I have been working since the late 1960s to elucidate properties of steroid hydroxylases and the development and maintenance of functional zonation of the adrenal cortex.
Immunohistochemical localization of steroid hydroxylases and establishment of the molecular basis for the functional zonation of the adrenal cortex
(1971) A specific role of reduced adrenodoxin in adrenal mitochondrial steroid hydroxylases. Biochem.
220.127.116.11, E20M) is the insect cytochrome P450-dependent steroid hydroxylase responsible for the conversion of the arthropod molting hormone ecdysone (E) to its more active metabolite, namely, 20-hydroxyecdysone (20E) [1, 2].
A number of plant allelochemicals, considered to have evolved to aid plants in their resistance to insect phytophagy, can affect insect steroid hydroxylase function [11-14].
Aside from the fact that the syntheses of anthraquinones permitted, for the first time, a study of chemical structure/function relationships as related to changes in E20M activity, they also permitted a first evaluation of the effects of these compounds on any steroid hydroxylase. Accordingly, an evaluation was pursued of the degrees to which quinizarin and five anthraquinone derivatives synthesized from quinizarin affect E20M activity in midgut tissues of the insect model, M.
Moreover, the present study represents the first demonstration that anthraquinones affect a P-450 dependent steroid hydroxylase in any invertebrate or vertebrate system.
Ecdysone 20-monooxygenase (E-20-M) is the cytochrome P-450 dependent steroid hydroxylase
responsible for the conversion of the insect molting hormone ecdysone (E) to its more physiologically active form 20-hydroxyecdysone (20-HE).
Novel involvement of a mitochondrial steroid hydroxylase
(P450c11) in xenobiotic metabolism.
Developmental expression of mouse steroidogenic factor-1, an essential regulator of the steroid hydroxylases
. Mol Endocrinol 8:654-662 (1994).
Analysis of the promoter regions of the genes encoding the steroid hydroxylases
has led to the identification of cAMP-responsive elements, but little is known about the mechanism through which PKA mediates the transcription of these target genes.