High impact information on NSC75895

• The ChPepz monomer effected hydrolysis of the ester group in N-benzoyl-L-tyrosine ethyl ester, an alpha-chymotrypsin substrate, with Km and kcat values that were comparable to those of alpha-chymotrypsin [1].
• Synthetic substrates for and an inhibitor of chymotrypsin-like proteases (e.g. N-benzoyl-L-tyrosine ethyl ester, L-1-tosylamido-2-phenylethyl chloromethyl ketone) also blocked O-2 release [2].
• Substrate specificities of each enzyme were further distinguished by use of benzoyl-L-tyrosine ethyl ester [3].
• The parameters measured were water, collagen, elastin, and glycosaminoglycan content; collagenase and elastase levels; and Bz-Tyr-OEt (N-benzoyl-L-tyrosine ethyl ester) and BAPNA (alpha-N-benzoyl-DL-arginine-p-nitroanilide) hydrolyzing activities [4].
• The pH optima for the major proteinases were determined to be pH 8.0-8.5 for trypsin, when tosyl-L-arginine methyl ester was used as the substrate; and pH 7.5-8.0 for chymotrypsin, when benzoyl-L-tyrosine ethyl ester was used as the substrate [5].

Biological context of NSC75895

• Changes in proteins from yolk and in the activity of benzoyl-L-tyrosine ethyl ester hydrolase from the yolk sac membrane during embryonic development of the chicken [6].

Anatomical context of NSC75895

• Purification and characterization of benzoyl-L-tyrosine ethyl ester hydrolase from the yolk sac membrane of chicken egg [7].

Gene context of NSC75895

• The immobilized enzyme showed favorable activity yields for both low- and high-mol-wt substrates, i.e., 90 +/- 9% for N-benzoyl-L-tyrosine ethyl ester and 59 +/- 5% for casein up to an enzyme coupling density of 0.38 g/g-PLS [8].

References