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Myo-inositol hexasulfate (MIHS), a structural analog of the substrate myo-inositol hexaphosphate, is a potent competitive inhibitor of both phyA and phyB enzymes. The Ki of inhibition for the phyA and phyB proteins were estimated to be 4.6 and 0.2 microM, respectively. Thus, the phyB protein is 23-fold more sensitive to MIHS inhibition than the phyA protein. The active-site geometry of phyB protein is presumed to be very different from the phyA protein as deduced by chemical probing of the enzymes by Arg-specific modifiers, i.e., 1,2-cyclohexanedione and phenylglyoxal. Probing the catalytic site of the same proteins by this newly developed specific inhibitor also gives a similar conclusion.
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