75396-30-4

Basic information

• Product Name: Lysine(butyryl)-OH
• Synonyms: Lysine(butyryl)-OH;H-Lys(Butyryl)-OH;N6-Butyryl-L-lysine
• CAS NO: 75396-30-4
• Molecular Formula: C10H20N2O3
• Molecular Weight: 216.28
• Mol File: 75396-30-4.mol
• Article Data: 3

Chemical Properties

• Boiling Point: 452.9±40.0 °C(Predicted)
• Appearance: /
• Density: 1.091±0.06 g/cm3(Predicted)
• PKA: 2.53±0.24(Predicted)
• CAS DataBase Reference: Lysine(butyryl)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Lysine(butyryl)-OH(75396-30-4)
• EPA Substance Registry System: Lysine(butyryl)-OH(75396-30-4)

Safety Data

• Hazardous Substances Data: 75396-30-4(Hazardous Substances Data)

Usage

General Description

Lysine(butyryl)-OH, also known as butyrylated lysine, is a modified form of the essential amino acid lysine. It is a derivative of lysine in which a butyryl group is attached to the amino acid. This modification can have various effects on the properties and functions of lysine in biological systems. Butyrylated lysine has been studied for its potential use in various applications, including as a dietary supplement, in food and beverage products, and in pharmaceutical formulations. It is also being researched for its potential therapeutic effects, particularly in the treatment of certain diseases and conditions. Overall, lysine(butyryl)-OH is a chemically modified form of lysine with potential applications in various fields.

Upstream product

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

Relevant articles and documents

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.

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.