126430-46-4Relevant articles and documents
PANTETHEINE DERIVATIVES AND USES THEREOF
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Paragraph 2121, (2020/06/19)
The present disclosure relates to compounds of Formula (I), (II), or (II'): (I), (II), (II'), and pharmaceutically acceptable salts or solvates thereof. The present disclosure also relates to pharmaceutical compositions comprising the compounds and therapeutic and diagnostic uses of the compounds and pharmaceutical compositions.
Cationic Lipid
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Paragraph 0189-0191, (2020/11/24)
The present invention provides a cationic lipid which is able to be used for nucleic acid delivery to the cytoplasm. A cationic lipid according to the present invention is, for example, a compound represented by formula (1) or a pharmaceutically acceptable salt thereof, wherein L1 and L2 independently represent an alkylene group having 3 to 10 carbon atoms; R1 and R2 independently represent an alkyl group having 4 to 24 carbon atoms or an alkenyl group having 4 to 24 carbon atoms; R3 represents an alkyl group having 1 to 3 carbon atoms; and X1 represents a single bond or CO—O—.
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.
