19361-52-5

Basic information

• Product Name: AC-PHE-TYR-NH2
• Synonyms: AC-PHE-TYR-NH2;(2S)-2-acetamido-N-[(2S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]-3-phenylpropanamide
• CAS NO: 19361-52-5
• Molecular Formula: C₂₀H₂₃N₃O₄
• Molecular Weight: 369.41
• Mol File: 19361-52-5.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: AC-PHE-TYR-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: AC-PHE-TYR-NH2(19361-52-5)
• EPA Substance Registry System: AC-PHE-TYR-NH2(19361-52-5)

Safety Data

• Hazardous Substances Data: 19361-52-5(Hazardous Substances Data)

Upstream product

• 2361-96-8 ethyl N-acetyl-(L)-phenylalaninate 
• 4985-46-0 L-Tyr-NH₂ 

Relevant articles and documents

Formation of amide bond catalyzed by lipase in aqueous phase for peptide synthesis

A dipeptide N-acetyl-l-phenylalanyl-l-tyrosinamide (N-Ac-Phe-Tyr-NH2), with angiotensin I converting enzyme (ACE) inhibitor activity, was synthesized via porcine pancreatic lipase catalyzed amidation of N-acetyl-phenylalanine ethyl ester with l-tyrosinamide in an aqueous phase. Response surface methodology was employed to evaluate the effects of synthesis parameters. The optimum synthesis conditions obtained an 84.45% yield of N-Ac-Phe-Tyr-NH2 with a reaction time of 3.8 min, a temperature of 20.9°C, an enzyme amount of 6.5 U, and a substrate molar ratio of 2.5:1 (Tyr:Phe). The kinetics of lipase and α-chymotrypsin catalyzed amidation was compared using the Ping-Pong mechanism. The lipase showed a lower apparent kinetic constant than α-chymotrypsin indicating that the acyl lipase intermediate had a higher affinity toward tyrosinamide in the amidation. In addition, because the lipase can avoid the secondary hydrolysis of synthesized peptide, it is expected to be an effective method for obtaining a good yield of dipeptide.