17331-91-8

Basic information

• Product Name: Z-TYR-LEU-NH2
• Synonyms: N-CARBOBENZOXY-L-TYROSYL-L-LEUCINE AMIDE;Z-TYR-LEU-NH2
• CAS NO: 17331-91-8
• Molecular Formula: C23H29N3O5
• Molecular Weight: 427.49
• Mol File: 17331-91-8.mol
• Article Data: 4

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: Z-TYR-LEU-NH2(CAS DataBase Reference)
• NIST Chemistry Reference: Z-TYR-LEU-NH2(17331-91-8)
• EPA Substance Registry System: Z-TYR-LEU-NH2(17331-91-8)

Safety Data

• Hazardous Substances Data: 17331-91-8(Hazardous Substances Data)

Usage

General Description

Z-TYR-LEU-NH2 is a synthetic chemical consisting of the amino acid sequence tyrosine (TYR), leucine (LEU), and an amide group (NH2). It is often used in research and drug development as a model compound to study the interactions and behavior of peptides in biological systems. Z-TYR-LEU-NH2 has been studied for its potential role in modulating neurotransmitter activity and as a potential therapeutic agent for conditions such as neurological disorders and chronic pain. Its chemical structure and properties make it a valuable tool for understanding the structure-activity relationships of peptides and for designing novel peptide-based drugs.

Upstream product

• 687-51-4 H-L-Leu-NH₂ 
• 16679-94-0 N-[(phenylmethoxy)carbonyl]-L-tyrosine 
• 13512-31-7 N-(benzyloxycarbonyl)-L-tyrosine methyl ester 
• 1164-16-5 Z-L-Tyr-OH 
• 15893-47-7 (R)-2-amino-4-methylpentanamide 
• 1668-11-7 2-Amino-4-methyl-pentanoic acid amide; hydrochloride 
• 13512-31-7 2-Benzyloxycarbonylamino-3-(4-hydroxy-phenyl)-propionic acid methyl ester 

Relevant articles and documents

Studies on Enzymatic Peptide Synthesis in Biphasic Aqueous-Organic Systems with Product Extraction

The dipeptide derivatives Z-Tyr-Leu-NH2 and Mca-Tyr-Leu-NH2 were synthesized by α-chymotrypsin-catalyzed coupling reactions in solvent systems consisting of buffer and ethyl acetate.In comparison to a pure aqueous medium, in which only insignificant synth

Enzymatic C-terminal amidation of amino acids and peptides

Herein, we describe two versatile and high yielding enzymatic approaches for the conversion of semi-protected amino acid and peptidyl C-terminal α-carboxylic acids into their corresponding amides. In the first approach, the lipase Candida antarctica lipase-B (Cal-B), and in the second approach, the protease Subtilisin A, are used, respectively. We found that by using the ammonium salt of the α-carboxylic acid instead of separate ammonia sources, the enzymatic amidation reactions proceeded much faster without side reactions and gave near to quantitative yields of products.