Fig. 1.

Summary of the AP active site. (a) Reaction scheme for the phosphomonoester hydrolysis catalyzed by AP. ROP and E-P represent the phosphate monoester substrate and covalent seryl-phosphate intermediate, respectively. (b) Schematic of the AP active site drawn with partial bonds as in the presumed phosphoryl-transfer transition state. (c) Inhibition constants were calculated for the AP•HPO${}_4^{2-}$ and AP•WO${}_4^{2-}$ complexes for select AP mutants at pH 8. From Andrews et al. [6].