Allosteric-Activation in Chymosin

What is it about?

We report the mechanism by which the aspartic protease enzyme, bovine chymosin, is allosterically activated by a HPHPH sequence from the milk protein, bovine κ-casein. Simulations performed independently using two different computational methods give the same allosteric activation mechanism, and additionally provide the free energy surface for the process. The simulations agree with previous kinetic, crystallographic and mutagenesis data, but they also provide molecular-scale data on the allosteric transition, which has thus far proven impossible to obtain using experimental methods.

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Why is it important?

Aspartic protease enzymes are important in many fields of research, including the food industry and pharmaceutical drug discovery. Chymosin itself is the most widely used enzyme in dairy food manufacturing; over 20.5 million metric tonnes of cheese alone are currently produced each year using the enzyme.