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Response to the Aids Pandemic
Published in Richard J. Sundberg, The Chemical Century, 2017
A third group of drugs are protease inhibitors (PIs). In the life cycle of HIV, the proteins synthesized by translation of the viral DNA are cleaved into smaller proteins by a protease. The HIV protease is called an aspartyl protease because its function depends upon an aspartic acid in the catalytic site. The protein structure was determined in 1988. It is a homodimer. It was also demonstrated in 1988 that inactivation of the protein led to immature, non-infectious virus particles. The three dimensional structure of this protease permitted the design and synthesis of inhibitors called peptidomimetics that are bound to the protease as if they were substrates, but which cannot be processed and inhibit the function of the enzyme (see Fig. 19.2). Promising structures were then synthesized and modified to address such issues as bioavailability, metabolic stability, and toxicity.
FRET Reporter Molecules for Identification of Enzyme Functions
Published in Grunwald Peter, Biocatalysis and Nanotechnology, 2017
Jing Mu, Hao Lun Cheong, Bengang Xing
Although aspartic protease has been found as the smallest class in the human genome, many of them have been treated as validated and potential drug targets in the pharmaceutical industry. Generally human aspartic proteases are divided into two clans based on their different tertiary structures: clan AA and clan AD (Eder et al., 2007). Clan AA contains the classical aspartic proteases (renin, pepsin A, pepsin C, cathepsin D, cathepsin E, BACE1, etc. Clan AD contains intra-membrane cleaving proteases like the presenilins and signal peptide peptidase.
Biochemical characterization of a partially purified protease from Aspergillus terreus 7461 and its application as an environmentally friendly dehairing agent for leather industry
Published in Preparative Biochemistry & Biotechnology, 2021
Emmly Ernesto de Lima, Daniel Guerra Franco, Rodrigo Mattos Silva Galeano, Nelciele Cavalieri de Alencar Guimarães, Douglas Chodi Masui, Giovana Cristina Giannesi, Fabiana Fonseca Zanoelo
Protease was strongly inhibited by PMSF, a synthetic serine protease inhibitor, widely used in biochemical studies to investigate the enzymatic mode of action.[48] Inhibition occurs due to sulfonation of the serine residue at the active site of the enzyme.[49,50] These results are similar to those described for A. terreus IJIRA 6.2[39], H. rhossiliensis OWVT-1[40], A. flavus[16] and A. brasiliensis.[36] On the other hand, the protease activity was not affected by the presence of the inhibitor pepstatin A, described in the literature as a competitive and reversible inhibitor of aspartic proteases.[51] Studies with the protease of P. aurantiogriseum have shown inhibition by PMSF and pepstatin A in 100 and 55%, respectively, suggesting that it is a serine protease with aspartic residues on its active site.[9] The data reported in this work confirm that the protease from A. terreus belongs to the class of serine proteases.
The high expression of Aspergillus pseudoglaucus protease in Escherichia coli for hydrolysis of soy protein and milk protein
Published in Preparative Biochemistry and Biotechnology, 2018
Haiyan Liu, Rongzhen Zhang, Lihong Li, Lixian Zhou, Yan Xu
Proteases (EC 3.4.11–24) catalyze the hydrolysis of peptide bonds in proteins.[7] According to their optimal pH values towards protein hydrolysis, the proteases are classified as acidic, neutral, and alkaline proteases. Acidic proteases, commonly known as aspartic proteases, widely existed in vertebrates, plants, fungi, bacteria, and viruses.[8] The acidic proteases are widely applied in different industries such as leather,[9] food,[10] beverage,[11,12] and pharmaceutical.[13] The acidic proteases are mainly applied in protein coagulation for cheese manufacturing and protein turbidity degradation in the beverage production.[8] At acid condition, the structure of the proteins may dissociate and become unfolded and this will enhance the hydrolysis efficiency.[14]