352431-48-2Relevant articles and documents
Synthesis of deuterium-labeled cinnamic acids: Understanding the volatile benzenoid pathway in the flowers of the Japanese loquat Eriobotrya japonica
Koeduka, Takao,Nishitani, Shiori,Watanabe, Bunta
, p. 403 - 416 (2021/08/09)
Cinnamic acids are widely distributed in plants, including crops for human use, and exhibit a variety of activities that are beneficial to human health. They also occupy a pivotal position in the biosynthesis of phenylpropanoids such as lignins, anthocyanins, flavonoids, and coumarins. In this context, deuterium-labeled cinnamic acids have been used as tracers and internal standards in food and medicinal chemistry as well as plant biochemistry. Therefore, a concise synthesis of deuterium-labeled cinnamic acids would be highly desirable. In this study, we synthesized deuterium-labeled cinnamic acids using readily available deuterium sources. We also investigated a hydrogen–deuterium exchange reaction in an ethanol-d1/Et3N system. This method can introduce deuterium atoms at the ortho and para positions of the phenolic hydroxy groups as well as at the C-2 position of alkyl cinnamates and is applicable to various phenolic compounds. Using the synthesized labeled compounds, we demonstrated that the benzenoid volatiles, such as 4-methoxybenzaldehyde, in the scent of the flowers of the Japanese loquat Eriobotrya japonica are biosynthesized from phenylalanine via cinnamic and 4-coumaric acids. This study provides easy access to a variety of deuterium-labeled (poly)phenols, as well as to useful tools for studies of the metabolism of cinnamic acids in living systems.
Stereochemistry and mechanism of a microbial phenylalanine aminomutase
Ratnayake, Nishanka Dilini,Wanninayake, Udayanga,Geiger, James H.,Walker, Kevin D.
supporting information; experimental part, p. 8531 - 8533 (2011/07/29)
The stereochemistry of a phenylalanine aminomutase (PAM) on the andrimid biosynthetic pathway in Pantoea agglomerans (Pa) is reported. PaPAM is a member of the 4-methylidene-1H-imidazol-5(4H)-one (MIO)-dependent family of catalysts and isomerizes (2S)-α-phenylalanine to (3S)-β-phenylalanine, which is the enantiomer of the product made by the mechanistically similar aminomutase TcPAM from Taxus plants. The NH2 and pro-(3S) hydrogen groups at Cα and Cβ, respectively, of the substrate are removed and interchanged completely intramolecularly with inversion of configuration at the migration centers to form β-phenylalanine. This is a contrast to the retention of configuration mechanism followed by TcPAM.
Mechanism leading to the observed product of intramolecular aryl Diels-Alder reaction
Chackalamannil, Samuel,Doller, Darío,Eagen, Keith
, p. 5101 - 5103 (2007/10/03)
A mechanistic investigation into the recently reported intramolecular aryl Diels-Alder reaction was carried out using deuterium labeling. These studies led to the conclusion that the initial Diels-Alder adduct is isomerized to a highly conjugated tetra-ene intermediate which undergoes a stereospecific suprafacial 1,5-dienyl hydrogen shift to give the observed product.
