Functional and immunological relationships between metyrapone reductase from mouse liver microsomes and 3α‐hydroxysteroid dehydrogenase from Pseudomonas testosteroni

Abstract

-HSD) from f?~domor~~s resroslerurri was shown to reduce the xenobiotic carbonyl compound mctyrapone (MPON). Revcrscly, MPON reductase purified from mouse liver microsomcs and previously characterized as aldehyde rcductase, was competitively inhibited by 3o-HSD steroid substrates. For MPON reduction both enzymes can use either NADH or NADPH as co-substrate. lmmunoblot analysis alter native and SDS gel eleclrophoresis of 31x-HSD gave a specific crossreaction with the antibodies against the microsomal mouse liver MPON reductase pointing to structural homologies bctwtin these enzymes. In conclusion, there seem to exist structural as well as functional relationships between a mammalian liver aldehyde reductase and prokaryotic 3a-HSD. Moreover, based on the molecular weights and the co-substrate specificities microsomal mouse liver MPON reductose and Pseudomonas 30.HSD seem to be members of the short-chain alcohol dehydrogenase fumily.

Characterization of a 3α‐Hydroxysteroid Dehydrogenase/Carbonyl Reductase from the Gram‐Negative Bacterium Comamonas testosteroni

“…The commercially available steroid-induced extract from C. testosterorzi ATCC 1 1 996 contains two enzymatically active protein bands with 3a-HSD and xenobiotic carbonyl reductase activity as assessed from native gel electrophoresis and as described previously [9]. The isolation of these two bands leads to two distinct proteins, which differ with respect to their migration behaviour in SDSIPAGE and immunoreactivity towards the mammalian type I 11P-HSD (cf.…”

Determination of 1-furan-2-yl-3-pyridin-2-yl-propenone, an anti-inflammatory propenone compound, by high performance liquid chromatography with ultraviolet spectrometry

“…Moreover, FPP-3 was rapidly converted to M1 and M2 within 2 min in biological fluids possibly by dehydrogenases or reductases present in liver and blood [5][6][7][8].…”

Regulation of the Steroid-inducible 3α-Hydroxysteroid Dehydrogenase/Carbonyl Reductase Gene in Comamonas testosteroni

“…To follow up our previous work on the molecular biology and structure of 3␣-HSD/CR (10,19,24,25,31), we investigated the transcriptional regulation of this important enzyme in C. testosteroni. In this study, we present the first data on the molecular mechanism of steroid induction in procaryotes.…”

“…Since the pioneering work of Marcus and Talalay (13), it is well known that 3␣-HSD is one of the first enzymes of the steroid catabolic pathway and that, therefore, it plays a central role in steroid metabolism. 3␣-HSD, which was first identified by its activity in converting dihydrocortisone to 3␣-tetrahydrocortisone (14), has been found in mammalian cells (15) and in procaryotes such as Clostridium perfringens (16), Eubacterium lentum (17), Pseudomonas putida (18), and C. testosteroni (10,19,20). Despite similar substrate specificities, eucaryotic and procaryotic 3␣-HSDs belong to two different protein superfamilies.…”