6665-12-9

Usage

Uses

Used in Pharmaceutical Industry:
L-Allysine is used as a pharmaceutical compound for its potential applications in drug development and therapeutic interventions. Its unique cyclic structure and properties make it a promising candidate for the treatment of various diseases and conditions.
Used in Biomedical Research:
L-Allysine is utilized as a research tool in biomedical studies, enabling scientists to explore its properties and potential applications in understanding biological processes and developing new therapies.
Used in Drug Synthesis:
L-Allysine is employed as a key intermediate in the synthesis of various pharmaceutical compounds, contributing to the development of new drugs and improving existing ones.
Used in Cosmetics Industry:
L-Allysine is used as an ingredient in cosmetics for its potential benefits in skin care and anti-aging products, thanks to its unique properties and ability to interact with biopolymers and macromolecules.

Upstream product

• 3105-95-1 pipecolinic acid 
• 73980-78-6 L-Δ¹-piperideine-6-carboxylic acid 

Downstream Products

• 997-68-2 L-Saccharopine 

Relevant academic research and scientific papers

Recreating the natural evolutionary trend in key microdomains provides an effective strategy for engineering of a thermomicrobial N-demethylase

N-demethylases have been reported to remove the methyl groups on primary or secondary amines, which could further affect the properties and functions of biomacromolecules or chemical compounds; however, the substrate scope and the robustness of N-demethylases have not been systematically investigated. Here we report the recreation of natural evolution in key microdomains of the Thermomicrobium roseum sarcosine oxidase (TrSOX), an N-demethylase with marked stability (melting temperature over 100 C) and enantioselectivity, for enhanced substrate scope and catalytic efficiency on -C-N-bonds. We obtained the structure of TrSOX by crystallization and X-ray diffraction (XRD) for the initial framework. The natural evolution in the nonconserved residues of key microdomains—including the catalytic loop, coenzyme pocket, substrate pocket, and entrance site—was then identified using ancestral sequence reconstruction (ASR), and the substitutions that accrued during natural evolution were recreated by site-directed mutagenesis. The single and double substitution variants catalyzed the N-demethylation of N-methyl-L-amino acids up to 1800- and 6000-fold faster than the wild type, respectively. Additionally, these single substitution variants catalyzed the terminal N-demethylation of non-amino-acid compounds and the oxidation of the main chain -C-N- bond to a -C=N- bond in the nitrogen-containing heterocycle. Notably, these variants retained the enantioselectivity and stability of the initial framework. We conclude that the variants of TrSOX are of great potential use in N-methyl enantiomer resolution, main-chain Schiff base synthesis, and alkaloid modification or degradation.