The study of Enzyme-Water Mutualism Theory

Document Type : Original Article


Biochemistry Department, School of Medicine, Universidad Autónoma de Madrid, Spain



A variety of experiments have shown that water can occur as a liquid of high and low density, with various physical characteristics, as the product of two kinds of hydrogen association between H20 molecules. This is essential intracellular, since solutes may favor a water type or other, creates local gradients of different waters behaviors which, due to volume restrictions, cannot be balanced by the flux but can be balanced by a shift between water shapes. It is quite probable that the developmental powers have manipulated this extraordinary water capacity, contributing to mutualism among adjacent H2O molecules and macromolecules. A consequence is a spectrum of substrate unique enzyme with macromolecular hydration, which enhances the catalysis, and hydrated by the more favorable ones of the two water configurations. Moreover, owing to selective isolation of enzyme reaction components, the variations in the water structure of low /high density purvey the pathway for protein folding; a basic requirement for enzyme functions without neglecting thermodynamics.