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-nitrophenyl phosphate, the common substrate for alkaline phosphatase (AP), is available as a cyclohexylamine salt. Here, we report that cyclohexylamine is a non-competitive inhibitor of APs. Cyclohexylamine inhibited four different APs. Co-crystallization with the cold-active AP (VAP) was performed and the structure solved. Inhibition of VAP fitted a non-competitive kinetic model (K unchanged, V reduced) with IC 45.3mMat the pH optimum 9.8, not sensitive to 0.5M NaCl, and IC 27.9mMat pH 8.0, where the addition of 0.5M NaCl altered the inh
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