Related Experiment Video
Updated: Jun 13, 2026

05:55
Identifying Inhibitors of the HBx-DDB1 Interaction Using a Split Luciferase Assay System
Published on: December 21, 2019
Peptidase inhibitors in the MEROPS database
1The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridgeshire CB10 1SA, UK. ndr@sanger.ac.uk
Biochimie
|May 1, 2010
Summary
The MEROPS database now includes small molecule inhibitors, crucial for characterizing peptidases and developing new drugs. This expansion aids researchers and the pharmaceutical industry in understanding enzyme interactions.
Area of Science:
- Biochemistry
- Pharmacology
- Bioinformatics
Background:
- The MEROPS database provides comprehensive information on peptidases, their substrates, and inhibitors.
- Protein peptidase inhibitors are classified into 67 families and 38 clans based on sequence and structural comparisons.
- Small molecule inhibitors are vital tools for peptidase research and drug development.
Purpose of the Study:
- To expand the MEROPS database to include small molecule inhibitors.
- To enhance the MEROPS website's functionality by linking peptidases and inhibitors.
- To provide updated classifications for protein peptidase inhibitors.
Main Methods:
- Curating and integrating data on small molecule inhibitors into the MEROPS database.
- Developing display features to link peptidases with their corresponding inhibitors.
- Classifying protein peptidase inhibitors based on sequence and tertiary structure comparisons.
Main Results:
- MEROPS now includes information on small molecule inhibitors, with over 160 summaries written.
- Enhanced displays facilitate the connection between peptidases and inhibitors.
- Protein inhibitors are organized into 67 families and 38 clans.
Conclusions:
- The inclusion of small molecule inhibitors significantly enhances the MEROPS database utility.
- MEROPS serves as a valuable resource for peptidase research and pharmaceutical development.
- The ongoing classification of inhibitors supports a deeper understanding of enzyme-inhibitor interactions.
Related Concept Videos
Dipeptidyl Peptidase 4 Inhibitors
Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a significant...
Inhibitors of Gram-positive Cell Wall Synthesis
Bacterial cell walls are typically rigid structures composed mainly of peptidoglycan, a mesh-like polymer that provides mechanical strength and maintains cell shape. The synthesis of peptidoglycan is a crucial process in bacterial growth and serves as a primary target for many antibiotics.Mechanism of Action of Beta-Lactam AntibioticsBeta-lactam antibiotics, such as penicillin, inhibit peptidoglycan synthesis in actively growing cells. These antibiotics share a characteristic four-membered...
Inhibitors of Bacterial Protein Synthesis
Aminoglycosides constitute a highly potent class of bactericidal antibiotics that exert their antimicrobial effects by targeting the bacterial ribosome, specifically disrupting protein synthesis. These polycationic molecules consist of amino-modified sugars linked via glycosidic bonds to an aminocyclitol core such as 2-deoxystreptamine or streptamine. Their strong positive charges facilitate tight binding to the negatively charged phosphate backbone of ribosomal RNA (rRNA), primarily at the 16S...
Enzyme Inhibition
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
Protein-protein Interfaces
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
