99051-65-7Relevant academic research and scientific papers
Cyanoalkyl difluoro-terphenyl-carboxylate chiral dopants
Kayani, Zohra N.,Lewis, Robert A.,Naseem, Shahzad
, p. 11 - 19 (2012)
A liquid crystal like difluoroterphenyl chiral dopant was synthesized to match the dimensions of a host chiral dopant mixture. The melting point of the chiral dopants was decreased by increasing the length of the alkyl chain. The melting point of the chiral dopants also decreased when fluorine was on the same ring as the ester i.e. at 2″, 3″ position. These dopants were formulated with terphenyl host mixture and liquid crystal properties were assessed. New dopants, when added to the host mixture, maintain SmA1 but the SmC2 phase was reduced markedly. There was a decrease in spontaneous polarisation when fluorine was on the same ring as the ester i.e. at 2″, 3″ position. As the molecular weight of the chiral dopant increased (pentyl ↑ heptyl ↑ nonyl), spontaneous polarisation decreased.
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases
Wada, Yusuke,Iwai, Saho,Tamura, Yusuke,Ando, Tomonori,Shinoda, Takeshi,Arai, Kazuhito,Taguchi, Hayao
, p. 1087 - 1094 (2008/09/21)
The gene for the D-mandelate dehydrogenase (DManDH) of Enterococcus faecalis IAM10071 was isolated by means of an activity staining procedure and PCR and expressed in Escherichia coli cells. The recombinant enzyme exhibited high catalytic activity toward various 2-ketoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-ketoisovalerate, and strict coenzyme specificity for NADH and NAD+. It showed marked sequence similarity with known NADP-dependent 2-ketopantoate reductases (KPR). These results indicate that together with KPR, D-ManDH constitutes a new family of D-2-hydroxyacid dehydrogenases that act on C3-branched 2-ketoacid substrates with various specificities for coenzymes and substrates.
