21394-43-4

Basic information

• Product Name: N-palmitoyl-L-methionine
• CAS NO: 21394-43-4
• Molecular Weight: 387.627
• Mol File: 21394-43-4.mol
• Article Data: 4

Chemical Properties

• CAS DataBase Reference: N-palmitoyl-L-methionine(CAS DataBase Reference)
• NIST Chemistry Reference: N-palmitoyl-L-methionine(21394-43-4)
• EPA Substance Registry System: N-palmitoyl-L-methionine(21394-43-4)

Safety Data

• Hazardous Substances Data: 21394-43-4(Hazardous Substances Data)

Upstream product

• 112-67-4 n-hexadecanoyl chloride 
• 10332-17-9 Met-OMe 
• 63-68-3 L-methionine 
• 1492-30-4 4-nitrophenyl palmitate 

Downstream Products

• 63-68-3 L-methionine 

Relevant articles and documents

MOLECULAR GELATORS FOR CONTAINING OIL SPILLAGE

The application relates to peptide-based compounds of Formula I such as the compound of Formula II, methods of making such compounds, gels comprising such compounds, methods of making gels, methods of using such compounds for containing the spill of a hydrocarbon, and methods for reclaiming solvent from gels comprising such compounds.

Purification, characterization, molecular cloning, and expression of a new aminoacylase from streptomyces mobaraensis that can hydrolyze N-(Middle/Long)-chain-fatty-acyl-L-amino acids as well as N-Short-chain-acyl-L- amino acids

We report here on the purification, characterization, molecular cloning, and expression of a new aminoacylase, initially isolated from the supernatant of Streptomyces mobaraensis (Sm-AA). Purified wild-type Sm-AA was found to be a monomeric protein with a molecular mass of 55 kDa. The cloned gene of Sm-AA contained an ORF of 1,383 bp, encoding a polypeptide of 460 amino acids. A BLAST search revealed that Sm-AA belongs to the peptidase M20 family, with identities to a hypothetical protein from Streptomyces pristinaespiralis, a putative peptidase from Streptomyces avermitilis, peptidase M20 from Frankia sp., succinyl-diaminopimelate desuccinylase from Hemophilus influenzae, and aminoacylase-1 from porcine kidney at 89, 88, 67, 29, and 25% respectively. The Sm-AA gene was subcloned into an expression vector, pSH19, and was expressed in Streptomyces lividans TK24. The amount of the recombi- nant Sm-AA expressed in the S. lividans cells was approximately 42-fold higher than that of Sm-AA found in the supernatant of S. mobaraensis. Sm-AA showed high hydrolytic activity towards various N-acetyl-L-amino acids and N-(middle/long)-chain-fatty-acyl-L- amino acids, with a preference for the acyl derivatives of L-Met, L-Ala, L-Cys, etc. with an optimum pH and temperature for reaction of about 7.5 and 50 °C (at pH 7.5).