Mass spectrometry of steroid systems—iv

Wulfson, N.S.; Zaretskii, V. I.; Sadovskaya, V. L.; Semenovsky, A. V.; Smit, W. A.; Kucherov, V. F.

doi:10.1016/0040-4020(66)80029-7

Cited by 23 publications

(3 citation statements)

References 3 publications

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“…High resolution mass measurement showed it to be approximately 85% Ci4H23+ (obsd 191.1796, caled 191.1800). This same fragment has been reported to be very prominent in the spectra of several terpanes isolated from petroleum (8-12) and several terpanes of known structure (11,(13)(14)(15)). It has usually been given ( 14) either of two structures (I, II) which, in this sample, could originate I II from different molecules or from different parts of the same molecule.…”

Section: Resultssupporting

confidence: 58%

Preparative thin-layer chromatography and high-resolution mass spectrometry of crude oil carboxylic acids

Seifert¹,

Teeter²

1969

Anal. Chem.

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Section: Resultssupporting

confidence: 58%

Preparative thin-layer chromatography and high-resolution mass spectrometry of crude oil carboxylic acids

Seifert¹,

Teeter²

1969

Anal. Chem.

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“…Steroids 4 and 5 are novel compounds, but 8 has a reported straightforward organic synthesis. Nevertheless, 8 ’s chemical properties are not published; no NMR structural data were released when it was initially isolated . Compounds 4 and 5 would have been difficult to produce by established methods.…”

Section: Figurementioning

confidence: 99%

Mammalian Cells Engineered To Produce New Steroids

et al. 2018

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Steroids can be difficult to modify via traditional organic synthesis methods, but many enzymes regio- and stereo-selectively process a wide variety of steroid substrates. We tested whether steroid-modifying enzymes could make novel steroids from non-native substrates. Numerous genes encoding steroid-modifying enzymes, including some bacterial enzymes, were expressed in mammalian cells by transient transfection and found to be active. We made three unusual steroids by stable expression in HEK293 cells of the 7α-hydroxylase CYP7B1, which was selected because of high native product yield. These cells made 7α,17α-dihydroxypregnenolone and 7β,17α-dihydroxypregnenolone from 17α-hydroxypregnenolone, and produced 11α, 16α-dihydroxyprogesterone from 16α-hydroxyprogesterone. The latter two products resulted from previously unobserved CYP7B1 hydroxylation sites. A Rosetta docking model of CYP7B1 suggested that these substrates’ D-ring hydroxylations may prevent them from binding in the same way as the native substrate, bringing different carbons near the active ferryl oxygen. This new approach could use other enzymes and substrates to produce many novel steroids for drug candidate testing.

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“…Nevertheless, 8's chemical properties are not published;n oN MR structurald ataw ere released when it was initially isolated. [27] Compounds 4 and 5 would have been difficult to produce by established methods. Both have been tentatively identified in mixtures of microbial steroid hydroxylation products, but no NMR data are available.…”

mentioning

confidence: 99%

Mammalian Cells Engineered to Produce Novel Steroids

Spady

Wyche

Rollins

et al. 2018

Preprint

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Steroids can be difficult to modify via traditional organic synthesis methods, but many enzymes regio-and stereo-selectively process a wide variety of steroid substrates. We tested whether steroid-modifying enzymes could make novel steroids from non-native substrates. Numerous genes encoding steroid-modifying enzymes, including some bacterial enzymes, were expressed in mammalian cells by transient transfection and found to be active. We made three unusual steroids by expression in HEK293 cells of the 7α-hydroxylase CYP7B1, which was selected because of high native product yield. These cells made 7α,17α-dihydroxypregnenolone and 7β,17α-dihydroxypregnenolone from 17α-hydroxypregnenolone, and produced 11α,16α-dihydroxyprogesterone from 16α-hydroxyprogesterone. The latter two products resulted from previously unobserved CYP7B1 hydroxylation sites. A Rosetta docking model of CYP7B1 suggested that these substrates' D-ring hydroxylations may prevent them from binding in the same way as the native substrate, bringing different carbons near the active ferryl oxygen. This new approach could use other enzymes and substrates to produce many novel steroids for drug candidate testing.

show abstract

Mass spectrometry of steroid systems—iv

Cited by 23 publications

References 3 publications

Preparative thin-layer chromatography and high-resolution mass spectrometry of crude oil carboxylic acids

Preparative thin-layer chromatography and high-resolution mass spectrometry of crude oil carboxylic acids

Mammalian Cells Engineered To Produce New Steroids

Mammalian Cells Engineered to Produce Novel Steroids

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