Disease relevance of Ethyl acetyltyrosinate

• N-Acetyl-L-tyrosine ethyl ester (ATEe) hydrolytic activities of diseased human palatine tonsils. Possible pathogenesis of recurrent acute tonsillitis [1].

High impact information on Ethyl acetyltyrosinate

• The irreversible proteinase inhibitor 3,4-dichloroisocoumarin (DCI) also blocked both chromium release and DNA fragmentation, but at significantly lower concentrations than ATEE [2].
• Both (2R,3S)- and (2S,3R)- delta EPhe-Phe(or Leu)-OMe were found to inhibit effectively the hydrolysis of Ac-Tyr-OEt by chymotrypsin in a competitive manner [3].
• But, in contrast to qBBr or methylation inhibitors, neither TEE nor ATEE was more effective when added prior to the initial effector-target interaction [4].
• Ac-Tyr-OEt, on the other hand, caused a marked accumulation of Ag-Ab complex in the lysosome fraction, reflecting the inhibition of intralysosomal digestion of the complex.(ABSTRACT TRUNCATED AT 250 WORDS)[5]
• When phagocytosis of the Ag-Ab complex was assayed by measuring the amount of digested products released from macrophage cells, Ac-Tyr-OEt also inhibited it as markedly as Ac-Phe-OEt, Ac-Trp-OEt, and Bz-Tyr-OEt did, whereas Bz-Arg-OEt again did not show any effect [5].

Biological context of Ethyl acetyltyrosinate

• A major ATEE site is very close to phosphorylation of the beta-subunit of the insulin receptor [6].
• The hydrolysis of ATEE by both free and encapsulated alpha-chymotrypsins apparently obeyed Michaelis-Menten kinetics [7].

Associations of Ethyl acetyltyrosinate with other chemical compounds

• The two reactions studied are the hydrolysis of ethyl N-acetyl-L-tyrosinate catalyzed by alpha-chymotrypsin and the acid-catalyzed hydrolysis of triethoxymethane [8].
• The pH optimum for the hydrolysis of N-acetyl-L-tyrosine ethyl ester (ATEE) by immobilized CT was higher than that of free CT [9].

Gene context of Ethyl acetyltyrosinate

• When the immobilized proteinase is exposed to 15 mM ethyl N-acetyl-L-tyrosinate in dilute pH 8.5 buffer it generates a microenvironment which, indicator studies suggest, has an effective pH of approximately 4 [10].
• It is based on the kinetic measurement of the C1 esterase-inhibitor when it inhibits the hydrolysis of N-acetyl-L-tyrosine-ethyl ester by C1 esterase [11].

References