40908-35-8

Usage

Uses

Used in Biochemical and Pharmaceutical Research:
Z-LEU-TYR-OH is used as a building block for the synthesis of peptides and proteins, facilitating the study of their structure and function, and contributing to the development of new drugs and therapies.
Used in Enzyme Assays:
Z-LEU-TYR-OH is used as a substrate in enzyme assays, allowing researchers to investigate the activity and specificity of enzymes involved in various biological processes.
Used as a Potential Therapeutic Agent:
Z-LEU-TYR-OH is utilized as a potential therapeutic agent for various diseases and disorders, offering new avenues for treatment and improving patient outcomes.

InChI:InChI=1/C23H28N2O6/c1-15(2)12-19(25-23(30)31-14-17-6-4-3-5-7-17)21(27)24-20(22(28)29)13-16-8-10-18(26)11-9-16/h3-11,15,19-20,26H,12-14H2,1-2H3,(H,24,27)(H,25,30)(H,28,29)

Upstream product

• 949-67-7 L-tyrosine ethyl ester 
• 2018-66-8 Z-Leu-OH 
• 17263-42-2 benzyl ((S)-1-(((S)-1-amino-3-(4-hydroxyphenyl)-1-oxopropan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)carbamate 

Downstream Products

• 1122069-35-5 Z-Leu-Tyr-Leu-OH 

Relevant academic research and scientific papers

Cross-linked crystals of subtilisin: Versatile catalyst for organic synthesis

Cross-linked enzyme crystals (CLECs) of subtilisin exhibit excellent activity in aqueous and various organic solvents. This catalyst is more stable than the native enzyme in both aqueous and mixed aqueous/organic solutions. Subtilisin-CLEC was shown to be a versatile catalyst. It was used for the syntheses of peptides and peptidomimetics, mild hydrolysis of amino acid and peptide amides, enantio- and regioselective reactions, and transesterifications.

Selectivity and Specificity in Substrate Binding to Proteases: Novel Hydrolytic Reactions Catalysed by α-Chymotrypsin Suspended in Organic Solvents with Low Water Content and Mediated by Ammonium Hydrogen Carbonate

α-Chymotrypsin suspended in organic solvents with low water content catalysed hydrolytic reactions in the presence of ammonium hydrogen carbonate.Molecular modelling studies were carried out and structure-reactivity relationships were established by studying the hydrolysis of amino acid derivatives and analogues.The enzyme was found to be stereoselective with respect to the hydrolysis of L-amino acid derivatives, but no stereoselectivity was observed when α-hydroxy esters were used as substrates.A general procedure for the resolution of aromatic amino acid esters is given.The results are interpreted in terms of molecular modelling based on X-ray crystallographic data and literature data.