The fleeting union of the enzyme and the substance on which it acts holds a key to our understanding of life processes. Many ingenious techniques are in use today to isolate it for study ...

The activation loop of the plasmin 'substrate', cleaved in these crystals, can be reconstructed to show how it runs across the active site of the plasmin 'enzyme' prior to activation cleavage.

Each enzyme molecule has a special place called the active site where another molecule, called the substrate, fits. The substrate goes through a chemical reaction and changes into a new molecule ...

However, it is safe to say that no enzyme is perfect in the sense of catalyzing only a single reaction with a single substrate. For enzymes such as P450s and glutathione S-transferases that are ...

The reaction requires short incubation times with small amounts of enzyme and is effective even at low substrate concentrations and at low temperatures. With these characteristics, it presents a ...

Deubiquitinases (DUBs) are enzymes used by cells to trim protein modifications made from the protein ubiquitin, and thereby ...

The rate of enzyme reaction can be affected by substrate concentration. As the substrate concentration increases, the enzyme reaction increases until all of the active sites are occupied by the ...

This causes the formation of more enzyme-substrate complexes, leading to an increase in enzyme activity. This means the active site loses its important shape and can no longer form enzyme ...

Functional assays showed that the enzyme dimer self-regulates through a mechanism called negative cooperativity. In this process, when a substrate binds to one-half (protomer) of the dimer ...

activity assays determined that GnT-IVa enzyme with GlcNAc glycan branches (higher binding) near the lectin domain decreases ...

Use a pair of plastic cuvettes, and start with the most dilute sample. 4. Prepare the substrate solution (3 tablets = 15 mg p-nitrophenylphosphate in 10 ml citrate buffer, = 5.5 mM). 5. Now you have ...