《Modulation of the catalytic properties of α-chymotrypsin by chemical modification at Tyr 146》 was published in Biochimica et Biophysica Acta, Protein Structure in 1978. These research results belong to Gorecki, Marian; Wilchek, Meir; Blumberg, Shmaryahu. Safety of H-D-Phe(4-NO2)-OMe.HCl The article mentions the following:
α-Chymotrypsin was modified with 3 different diazonium salts derived from D-phenylalanine. All 3 reagents reacted selectivity with tyrosine-146 on the surface of the enzyme. The spectral and enzymic properties of the azochymotrypsins were characteristic for each of the proteins. Depending on the structure of the reagent used for modification, the activity towards p-nitroanilide substrate was higher or about the same as that of the native enzyme. In addition to this study using H-D-Phe(4-NO2)-OMe.HCl, there are many other studies that have used H-D-Phe(4-NO2)-OMe.HCl(cas: 67877-95-6Safety of H-D-Phe(4-NO2)-OMe.HCl) was used in this study.
H-D-Phe(4-NO2)-OMe.HCl(cas: 67877-95-6) belongs to esters. Esters are more polar than ethers but less polar than alcohols. Safety of H-D-Phe(4-NO2)-OMe.HCl They participate in hydrogen bonds as hydrogen-bond acceptors, but cannot act as hydrogen-bond donors, unlike their parent alcohols. This ability to participate in hydrogen bonding confers some water-solubility.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics