112100-39-7Relevant articles and documents
Straightforward and efficient synthesis of (4R,6S)-4-(tert-butyldimethyl- siloxy)-6-(hydroxymethyl)tetrahydropyran-2-one
?asar, Zdenko
, p. 2036 - 2040 (2008)
A novel synthetic approach to (4R,6S)-4-(tert-butyldimethylsiloxy)-6- (hydroxymethyl)tetrahydropyran-2-one, a key precursor of statin side chain, is described. A prime feature of the presented strategy is the transformation of (4R,6S)-4-(tert-butyldimethylsiloxy)-6-(iodomethyl)tetrahydropyran-2-one to an acetate ester derivative and subsequent cleavage of an acetate protection by applying homogeneous tin catalysis. Iodolactone used in the study is accessible by a new route in five steps from (S)-ethyl 4-chloro-3-hydroxybutanoate. This method overcomes many of the drawbacks associated with previously reported approaches. It gives the title compound in 21% over seven steps, which is the highest attained overall yield yet. The disclosed approach was realized in convenient and economical manner suitable for industrial use.
SUBSTITUTED STRAIGHT CHAIN SPIRO DERIVATIVES
-
Page/Page column 115, (2021/06/26)
Provided herein are pharmaceutical agents useful for therapy and/or prophylaxis in a mammal, pharmaceutical composition comprising such compounds, and their use as menin/MLL protein/protein interaction inhibitors, useful for treating diseases such as cancer, including but not limited to leukemia, myelodysplastic syndrome (MDS), and myeloproliferative neoplasms (MPN); and diabetes.
Cation-π interactions contribute to substrate recognition in γ-butyrobetaine hydroxylase catalysis
Kamps, Jos J. A. G.,Khan, Amjad,Choi, Hwanho,Lesniak, Robert K.,Brem, Jürgen,Rydzik, Anna M.,McDonough, Michael A.,Schofield, Christopher J.,Claridge, Timothy D. W.,Mecinovic, Jasmin
supporting information, p. 1270 - 1276 (2016/01/25)
γ-Butyrobetaine hydroxylase (BBOX) is a non-heme FeII- and 2-oxoglutarate-dependent oxygenase that catalyzes the stereoselective hydroxylation of an unactivated C-H bond of γ-butyrobetaine (γBB) in the final step of carnitine biosynthesis. BBOX contains an aromatic cage for the recognition of the positively charged trimethylammonium group of the γBB substrate. Enzyme binding and kinetic analyses on substrate analogues with P and As substituting for N in the trimethylammonium group show that the analogues are good BBOX substrates, which follow the efficiency trend N+>P+>As+. The results reveal that an uncharged carbon analogue of γBB is not a BBOX substrate, thus highlighting the importance of the energetically favorable cation-π interactions in productive substrate recognition. What's in the BBOX? Enzyme kinetics and substrate binding studies reveal that γ-butyrobetaine hydroxylase (BBOX)-catalyzed stereoselective hydroxylation of γ-butyrobetaine involves energetically favorable cation-π interactions.
