75396-30-4

Usage

Uses

Used in Dietary Supplements:
Lysine(butyryl)-OH is used as a dietary supplement to provide the body with an enhanced form of the essential amino acid lysine. The butyryl group attached to lysine may offer additional benefits, such as improved absorption and utilization by the body.
Used in Food and Beverage Products:
Lysine(butyryl)-OH is used in food and beverage products to fortify them with an enhanced form of lysine. This can help improve the nutritional profile of these products and provide consumers with additional health benefits.
Used in Pharmaceutical Formulations:
Lysine(butyryl)-OH is used in pharmaceutical formulations for its potential therapeutic effects. The butyryl group attached to lysine may enhance the bioavailability and efficacy of the amino acid, making it a valuable component in the development of new drugs and treatments.
Used in the Treatment of Certain Diseases and Conditions:
Lysine(butyryl)-OH is being researched for its potential therapeutic effects in the treatment of certain diseases and conditions. The modified form of lysine may offer unique benefits in addressing specific health issues, making it a promising candidate for further study and development in the medical field.

Upstream product

• 106-31-0 butanoic acid anhydride 
• 657-27-2 L-Lysine hydrochloride 
• 56-87-1 L-lysine 
• 107-92-6 butyric acid 
• 13734-28-6 Boc-Lys-OH 
• 141-75-3 butyryl chloride 
• 105-60-2 caprolactam 

Relevant academic research and scientific papers

Repurposing the 3-Isocyanobutanoic Acid Adenylation Enzyme SfaB for Versatile Amidation and Thioesterification

Genome mining of microbial natural products enables chemists not only to discover the bioactive molecules with novel skeletons, but also to identify the enzymes that catalyze diverse chemical reactions. Exploring the substrate promiscuity and catalytic mechanism of those biosynthetic enzymes facilitates the development of potential biocatalysts. SfaB is an acyl adenylate-forming enzyme that adenylates a unique building block, 3-isocyanobutanoic acid, in the biosynthetic pathway of the diisonitrile natural product SF2768 produced by Streptomyces thioluteus, and this AMP-ligase was demonstrated to accept a broad range of short-chain fatty acids (SCFAs). Herein, we repurpose SfaB to catalyze amidation or thioesterification between those SCFAs and various amine or thiol nucleophiles, thereby providing an alternative enzymatic approach to prepare the corresponding amides and thioesters in vitro.

Synthesis of ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine containing histone H3 using the pyrrolysine system

Recently new lysine modifications were detected in histones and other proteins. Using the pyrrolysine amber suppression system we genetically inserted three of the new amino acids ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine site specifically int

Molecular rotations of N(α)-acyl-L-lysines at various pH values

Molecular rotations of N(α)-acyl-L-lysines were determined in water and in water containing various amounts of HCl or NaOH. The acyl groups were formyl, acetyl, propionyl, and butyryl. Each N(α)-acyl-L-lysine exhibited more negative rotation in HCl or NaOH solution than in water. The plot of molecular rotation against amount of HCl or NaOH resembled that of a D-α-amino acid even though N(α)-acyl-lysine was of L-form. The reason for this is discussed from the standpoint of steric factors. N(ε)-Acyl-L-lysines corresponding to the N(α)-acyl-L-lysines were synthesized as reference compounds. It was found that water-soluble N(ε)-acyl-L-lysines can be easily prepared by acylation of the Cu complex solution of L-lysine hydrochloride in the presence of triethylamine. The molecular rotation plots for N(ε)-acyl-L-lysines were typical of L-α-amino acids.