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Usage

Uses

Used in Pharmaceutical Industry:
L-Glutamic acid, N-[(phenylmethoxy)carbonyl]-, 1-1-methylethyl) ester is used as a key intermediate in the synthesis of various pharmaceuticals for its ability to facilitate the creation of complex organic molecules and peptides that are vital for drug development.
Used in Agrochemical Industry:
In the agrochemical sector, L-Glutamic acid, N-[(phenylmethoxy)carbonyl]-, 1-1-methylethyl) ester is utilized as a component in the production of agrochemicals, contributing to the development of effective and targeted crop protection products.
Used in Fine Chemicals Production:
L-Glutamic acid, N-[(phenylmethoxy)carbonyl]-, 1-1-methylethyl) ester is employed as a versatile precursor in the synthesis of fine chemicals, where its reactivity and functional groups are harnessed to produce high-quality specialty chemicals for various applications.
Used in Organic Synthesis:
As a fundamental building block in organic synthesis, L-Glutamic acid, N-[(phenylmethoxy)carbonyl]-, 1-1-methylethyl) ester is used for the preparation of a diverse array of organic compounds, showcasing its adaptability and importance in chemical research and development.

InChI:InChI=1/C16H21NO6/c1-11(2)23-15(20)13(8-9-14(18)19)17-16(21)22-10-12-6-4-3-5-7-12/h3-7,11,13H,8-10H2,1-2H3,(H,17,21)(H,18,19)/t13-/m0/s1

Upstream product

• 5672-83-3 Z-L-GluOMe 
• 67-63-0 isopropyl alcohol 

Relevant academic research and scientific papers

PEPTIDE SYNTHESIS CATALYZED BY NATIVE PROTEINASE K IN WATER-MISCIBLE ORGANIC SOLVENTS WITH LOW WATER CONTENT

Rection of Ac-Tyr-OEt with HBr.Gly-NH2, catalysed by free proteinase K in various water-miscible organic solvents in the presence of triethylamine and 5 mol percent of water, was studied.Some aliphatic alcohols and acetonitrile proved to be suitable solvents.The effect of water content (2 percent - 20 percent) on the synthesis of Ac-Tyr-Gly-NH2 was studied using acetonitrile as solvent.Lowering of the water content to 5 percent or 2 percent led to almost 100 percent yield of the desired dipeptide; higher water content accelerated the reaction reducing at the same time the yield of Ac-Tyr-Gly-NH2 due to the concurrent hydrolysis of the ester Ac-Tyr-OEt.No reaction was observed in the absence of base (triethylamine), wereas an excess of base only retarded the reaction.The enzyme is capable of catalyzing the peptide bond synthesis with N-acylamino acids or N-acyl peptides as acylating components, which may contain all types of L-amino acid residues (except Pro) in the P1 position.However, the peptide bond synthesis depends strongly on the amino component composition, particularly on the amino acid residue in the P'1 position.Only amides of glycine and of hydrophillic amino acids were acylated with Ac-Tyr-OEt; amides of hydrophobic amino acids enter the reaction only reluctantly or not at al.The presence of Leu or Phe in position P'2 and Leu in position P'3 has not so negative effect on acylation of the amino component as has in presence in the P'1 position.The choice of protecting groups for the α-carboxyl of the amino component is restricted only to amide and in some cases its undesired enzymatic removal was observed.Unprotected peptides seem to be suitable amino components.