1962-83-0

Usage

Uses

Used in Pharmaceutical Industry:
L-2-AMINOADIPATE 6-SEMIALDEHYDE is used as an intermediate compound for the synthesis of various pharmaceutical products. Its unique structure allows it to be a key component in the development of new drugs targeting specific metabolic pathways and conditions.
Used in Research and Development:
In the field of research and development, L-2-AMINOADIPATE 6-SEMIALDEHYDE serves as an essential compound for studying the metabolic pathways involving lysine and its derivatives. It can be used to investigate the role of L-2-AMINOADIPATE 6-SEMIALDEHYDE in various biological processes and its potential as a therapeutic agent.
Used in Nutritional Supplements:
L-2-AMINOADIPATE 6-SEMIALDEHYDE can be utilized as an ingredient in nutritional supplements, particularly those aimed at supporting lysine metabolism and overall health. Its presence in these supplements may contribute to the maintenance of proper metabolic function and the enhancement of certain physiological processes.
Used in Cosmetics Industry:
The unique properties of L-2-AMINOADIPATE 6-SEMIALDEHYDE may also find applications in the cosmetics industry, where it can be used as an active ingredient in skincare and hair care products. Its potential role in promoting skin health and improving the appearance of hair could make it a valuable addition to various cosmetic formulations.

InChI:InChI=1/C6H11NO3/c7-5(6(9)10)3-1-2-4-8/h4-5H,1-3,7H2,(H,9,10)

Upstream product

• 170242-34-9 α-aminoadipate semialdehyde ethyleneacetal 

Relevant academic research and scientific papers

Role and structural characterization of plant aldehyde dehydrogenases from family 2 and family 7

Aldehyde dehydrogenases (ALDHs) are responsible for oxidation of biogenic aldehyde intermediates as well as for cell detoxification of aldehydes generated during lipid peroxidation. So far, 13 ALDH families have been described in plants. In the present study, we provide a detailed biochemical characterization of plant ALDH2 and ALDH7 families by analysing maize and pea ALDH7 (ZmALDH7 and PsALDH7) and four maize cytosolic ALDH(cALDH)2 isoforms RF2C, RF2D, RF2E and RF2F [the first maize ALDH2 was discovered as a fertility restorer (RF2A)]. We report the crystal structures of ZmALDH7, RF2C and RF2F at high resolution. The ZmALDH7 structure shows that the three conserved residues Glu120 , Arg300 and Thr302 in the ALDH7 family are located in the substrate-binding site and are specific to this family. Our kinetic analysis demonstrates that α -aminoadipic semialdehyde, a lysine catabolism intermediate, is the preferred substrate for plant ALDH7. In contrast, aromatic aldehydes including benzaldehyde, anisaldehyde, cinnamaldehyde, coniferaldehyde and sinapaldehyde are the best substrates for cALDH2. In line with these results, the crystal structures of RF2C and RF2F reveal that their substrate-binding sites are similar and are formed by an aromatic cluster mainly composed of phenylalanine residues and several nonpolar residues. Gene expression studies indicate that the RF2C gene, which is strongly expressed in all organs, appears essential, suggesting that the crucial role of the enzyme would certainly be linked to the cellwall formation using aldehydes from phenylpropanoid pathway as substrates. Finally, plant ALDH7 may significantly contribute to osmoprotection because it oxidizes several aminoaldehydes leading to products known as osmolytes.