N-Acetyl-L-tyrosine ethyl ester monohydrate has been used:
as a substrate in transesterification reactions with 1 M propan-1-ol catalyzed by Carlsberg protease protein-coated microcrystals (PCMC)[1]
to test the performance of subtilisin Carlsberg protein-coated microcrystals (PCMC)[2]
as a substrate for cross-linked crystals (CLECs) of subtilisin activity screening[3]
Biochem/physiol Actions
N-Acetyl-L-tyrosine ethyl ester is an N-terminal and C-terminal protected L-tyrosine that is used in crosslinking studies and as a substrate for the detection, differentiation and/or characterization various proteases and esterases.
To evaluate if unconjugated bilirubin (UB) inhibits C1 esterase activity. Esterase activity was evaluated by C1-mediated hydrolysis of N-acetyl-L-tyrosine ethyl ester, and binding of UB to C1r and C1s was assessed by dot-blot analysis. UB inhibited C1 enzymatic activity. C1r
Stability of protein-coated microcrystals in organic solvents
Kreiner M, et al.
Journal of Molecular Catalysis. B, Enzymatic, 33(3-6) (33)
Operational stability of subtilisin CLECs in organic solvents in repeated batch and in continuous operation
Fernandes JFA, et al.
Biochemical Engineering Journal, 24(1) (24)
A study of the intermolecular interactions of tolmetin/N-acetyl-L-tyrosine ethyl ester complex.
Tito A, Jimenez-Lopez C, et al.
Spectrochimica Acta Part A: Molecular Spectroscopy, 72, 1000-1006 (2009)
The crystal structure of a protected L-tyrosine, namely N-acetyl-L-tyrosine methyl ester monohydrate, C(12)H(15)NO(4).H(2)O, was determined at both 293 (2) and 123 (2) K. The structure exhibits a network of O-H...O and N-H...O hydrogen bonds, in which the water molecule plays
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.