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Catalytic Mechanism of SARS-CoV-2 3-Chymotrypsin-Like Protease as Determined by Steady-State and Pre-Steady-State Kinetics.
ACS Catal
December 2024
Departments of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States.
Article Synopsis
- The 3-chymotrypsin-like protease (3CL-PR) of SARS-CoV-2 is essential for virus replication and is targeted by the COVID-19 drug Paxlovid, making it important for understanding its catalytic behavior.
- Research indicates that the activity of 3CL-PR is pH-dependent, with specific acidic and basic groups necessary for optimal enzymatic function, suggesting a neutral catalytic dyad involving cysteine and histidine.
- Kinetic studies reveal faster rates in certain conditions, highlighting the influence of the active form of the enzyme, and a full catalytic mechanism for 3CL-PR is proposed based on these findings.
Validation of Molecular Markers for Low Kunitz Trypsin Inhibitor Content in European Soybean ( L. Merr.) Germplasm.
Genes (Basel)
August 2024
Faculty of Agriculture, University of Zagreb, Svetošimunska Cesta 25, 10000 Zagreb, Croatia.
Trypsin inhibitors (TI) in raw soybean grain, mainly represented by the Kunitz trypsin inhibitor protein (KTI), prevent the normal activity of the digestive enzymes trypsin and chymotrypsin in humans and monogastric livestock. The inactivation of TI is achieved through costly and time-consuming heat treatment. Thermal processing also impairs the solubility and availability of the soybean grain protein.
View Article and Find Full Text PDFSecretagogue-induced pancreatitis in mice devoid of chymotrypsin.
Am J Physiol Gastrointest Liver Physiol
September 2024
Department of Surgery, University of California Los Angeles, Los Angeles, California, United States.
The serine protease chymotrypsin protects the pancreas against pancreatitis by degrading trypsinogen, the precursor to the digestive protease trypsin. Taking advantage of previously generated mouse models with either the gene (encoding chymotrypsin B1) or the gene (encoding chymotrypsin-like protease) disrupted, here we generated the novel × strain in the C57BL/6N genetic background, which harbors a naturally inactivated gene (encoding chymotrypsin C). The newly created mice are devoid of chymotrypsin, yet the animals develop normally, breed well, and show no spontaneous phenotype, indicating that chymotrypsin is dispensable under laboratory conditions.
View Article and Find Full Text PDFBowman-Birk Inhibitor Mutants of Soybean Generated by CRISPR-Cas9 Reveal Drastic Reductions in Trypsin and Chymotrypsin Inhibitor Activities.
Int J Mol Sci
May 2024
Plant Genetics Research Unit, US Department of Agriculture-Agricultural Research Service, Columbia, MO 65211, USA.
Despite the high quality of soybean protein, raw soybeans and soybean meal cannot be directly included in animal feed mixtures due to the presence of Kunitz (KTi) and Bowman-Birk protease inhibitors (BBis), which reduces animal productivity. Heat treatment can substantially inactivate trypsin and chymotrypsin inhibitors (BBis), but such treatment is energy-intensive, adds expense, and negatively impacts the quality of seed proteins. As an alternative approach, we have employed CRISPR/Cas9 gene editing to create mutations in genes to drastically lower the protease inhibitor content in soybean seed.
View Article and Find Full Text PDFPurification and partial physical-chemical characterization of a new bovine trypsin proteoform (zeta-trypsin).
Int J Biol Macromol
May 2024
Pos-Graduate Program of Biotechnology - Federal University of Espírito Santo, Vitória, ES, Brazil; Pos-Graduate Program of Biochemistry - Federal University of Espírito Santo, Vitória, ES, Brazil. Electronic address:
Recent advancements in enzyme research have unveiled a new proteoform of bovine trypsin, expanding our understanding of this well-characterized enzyme. While generally similar to other trypsins, this novel proteoform comprises three polypeptide chains, marking a significant difference in activity, kinetic properties, and conformational stability. Compared with the already known bovine trypsin proteoforms, the results showed a lower: activity, k and k.
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