Phenylhydrazide as an enzyme-labile protecting group in peptide synthesis was written by Voelkert, Martin;Koul, Surrinder;Mueller, Gernot H.;Lehnig, Manfred;Waldmann, Herbert. And the article was included in Journal of Organic Chemistry in 2002.Quality Control of Ethyl 2-hydroxy-3-phenylpropanoate This article mentions the following:
The enzymic cleavage of amino acid phenylhydrazides with the enzyme tyrosinase (EC 1.14.18.1) offers a new, mild, and selective method for C-terminal deprotection of peptides. The advantages of the described methodol. are the very mild oxidative removal of the protecting group at room temperature and pH 7, a high chemo- and regioselectivity, and the availability of the biocatalyst. Even in oxygen-saturated solution, the oxidation of sensitive methionine residues was not observed These features make the methodol. suitable for the synthesis of sensitive peptide conjugates. Mechanistic data suggest that the hydrolysis of the oxidized adducts proceeds by a free-radical mechanism. In the experiment, the researchers used many compounds, for example, Ethyl 2-hydroxy-3-phenylpropanoate (cas: 15399-05-0Quality Control of Ethyl 2-hydroxy-3-phenylpropanoate).
Ethyl 2-hydroxy-3-phenylpropanoate (cas: 15399-05-0) belongs to esters. Esters are widespread in nature and are widely used in industry. In nature, fats are in general triesters derived from glycerol and fatty acids. Esters are responsible for the aroma of many fruits. Because of their lack of hydrogen-bond-donating ability, esters do not self-associate. Consequently, esters are more volatile than carboxylic acids of similar molecular weight.Quality Control of Ethyl 2-hydroxy-3-phenylpropanoate
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics