The shikimate pathway is fundamental for the biosynthesis of aromatic amino acids—tryptophan, tyrosine and phenylalanine—in plants, bacteria and fungi. This pathway, which is absent in mammals, has ...

Enzyme activity is commonly controlled by allostery, where ligand binding at one site alters the activities of distant sites. Classical explanations for multisubunit proteins involve conformational ...

One of the key features in the evolution of more complex organisms is the emergence of allosteric regulation. Allostery is a process by which a protein’s activity can be modulated by binding an ...

The speed at which an enzyme catalyzes a reaction typically doubles with every 10 °C increase in temperature. But analogous enzymes found in tropical fish and Arctic fish tend to work at the same rate ...

Most proteins comprise two or more domains from a limited suite of protein families. These domains are often rearranged in various combinations through gene fusion events to evolve new protein ...

Allostery refers to the binding of a metabolite at a site other than the chemically active site of a protein. The existence of allosteric sites on receptor molecules has expanded potential drug ...

A new study is changing how researchers look at diabetes research and the drugs used to treat the disease. Researchers report that a key enzyme involved in the body's response to glucose can ...

The first full-length structures of the human angiotensin-converting enzyme (ACE) have been determined by researchers from the University of Cape Town (UCT) using cryo-electron microscopy (cryo-EM).

The first full-length structures of the human angiotensin-converting enzyme (ACE) have been determined by researchers from the University of Cape Town (UCT) using cryo-electron microscopy (cryo-EM).

TALLAHASSEE, Fla. -- A new Florida State University study is changing how researchers look at diabetes research and the drugs used to treat the disease. In today's issue of the Proceedings of the ...