70497-50-6

Basic information

• Product Name: N-[(benzyloxy)carbonyl]alanylvalinamide
• CAS NO: 70497-50-6
• Molecular Formula: C₁₆H₂₃N₃O₄
• Molecular Weight: 321.3715
• Mol File: 70497-50-6.mol

Chemical Properties

• Boiling Point: 593.2°C at 760 mmHg
• Flash Point: 312.6°C
• Density: 1.17g/cm³
• Vapor Pressure: 4.83E-14mmHg at 25°C
• Refractive Index: 1.533
• CAS DataBase Reference: N-[(benzyloxy)carbonyl]alanylvalinamide(CAS DataBase Reference)
• NIST Chemistry Reference: N-[(benzyloxy)carbonyl]alanylvalinamide(70497-50-6)
• EPA Substance Registry System: N-[(benzyloxy)carbonyl]alanylvalinamide(70497-50-6)

Safety Data

• Hazardous Substances Data: 70497-50-6(Hazardous Substances Data)

Upstream product

• 28819-05-8 (S)-2-benzyloxycarbonylamino-propionic acid methyl ester 
• 3014-80-0 (S)-2-amino-3-methylbutanamide hydrochloride 
• 4816-87-9 Z-L-Ala carbamoylmethyl ester 
• 60625-90-3 Cbz-alanine ethyl ester 
• 203640-41-9 Z-L-Ala 2,2,2-trifluoroethyl ester 
• 1142-20-7 N-Cbz-Ala 

Relevant articles and documents

Mechanoenzymatic peptide and amide bond formation

Mechanochemical chemoenzymatic peptide and amide bond formation catalysed by papain was studied by ball milling. Despite the high-energy mixing experienced inside the ball mill, the biocatalyst proved stable and highly efficient to catalyse the formation of α,α- and α,β-dipeptides. This strategy was further extended to the enzymatic acylation of amines by milling, and to the mechanosynthesis of a derivative of the valuable dipeptide L-alanyl-l-glutamine.

Superiority of the carbamoylmethyl ester as an acyl donor for the kinetically controlled amide-bond formation mediated by α-chymotrypsin

The superiority of the carbamoylmethyl ester as an acyl donor for the α-chymotrypsin-catalysed kinetically controlled peptide-bond formation is demonstrated in the couplings of an inherently poor amino acid substrate, Ala, with various amino acid residues as amino components and in the couplings of non-protein amino acids such as halogenophenylalanines as carboxylic components. Furthermore, this approach is applied to the amide-bond formation between an amino acid residue and a chiral amine, which is highly diastereoselective.

Pronase catalysed peptide syntheses

A mixture of proteases from Streptomyces griseus (pronase), displaying a very broad substrate tolerance in the hydrolysis of peptides, has been studied for the first time systematically regarding their substrate specificity in peptide synthesis. It is demonstrated that pronase can be employed successfully for the formation of dipeptides with yields up to 95%. Pronase has also been employed successfully as catalyst for the enzyme assisted synthesis of a hexapeptide.