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.
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
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)
Biotechnology and bioengineering, 87(1), 24-33 (2004-06-24)
Recently, we reported a new high-activity biocatalyst for use in organic media termed protein-coated microcrystals (PCMC) (Kreiner et al. [2001] Chem Commun 12:1096-1097). These novel particles consist of water-soluble micron-sized crystalline particles coated with the given biocatalyst(s) and are prepared
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