Abstract
Summary The catalytic mechanism of the serine proteases as currently conceived specifies that the charge relay system Asp is ionized at pH's where the enzymes are active. This choice is questioned on the basis that external anions are found associated with the charge relay system of both chymotrypsin and subtilisin at pH's below the charge relay system pK, and no evidence has been found for the presence of an associated cation at pH's above the charge relay system pK. An alternative catalytic mechanism is proposed wherein Nδl of the His imidazole is hydrogen bonded to a neutral Asp, and His-Nɛ2 functions to relay a proton from Ser-Oγ to the substrate in a manner analogous to proton transfer in ice.
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