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 ...

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 ...

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

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.

The process of an enzyme breaking a substrate molecule apart. If enzymes are heated too much or put into a higher or lower pH, their shape can change. The enzyme undertakes a process of ...

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 ...

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 ...

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 ...

Enzymes that catalyze the reaction of transferring phosphate groups to proteins using adenosine triphosphate as a substrate are called protein kinases, and enzymes that catalyze the reaction of ...