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Background

Phosphatase enzymes catalyze the hydrolysis of the phosphate group off of a phosphoric monoester. The R-group of the phosphate monoester is removed and then forms a new bond with an O-H molecule derived from water. The remaining hydrogen left over from the water molecule bonds to the oxygen on the phosphate group, which was once bonded to the R-group. Phosphatases can be categorized as either “alkaline or “acidic” depending on the enzyme’s optimal pH. Alkaline phosphatases will initiate catalytic activity at a pH above 7 and acidic phosphatases will have a higher catalytic activity at a pH lower than 7. Dephosphorylation of macromolecules such as nucleotides or proteins during catabolic processes is essential when maintaining homeostasis within a cell or during cell signaling. As previously stated, acid phosphatases work in acidic environments and can be found throughout the human body. Phosphatases may also be either intracellular or extracellular. Intracellular phosphatases can be found in the kidneys, spleen, liver, bloodstream and plant tissues. Whereas extracellular phosphatases can be found in soil and water which help with biogeochemical cycling of phosphorus and organic phosphorus intake in plants (Pant 2014).

Structure

Acid phosphatases’ secondary structure is composed of 15% alpha helices (11 helices; 69 residues) and 29% beta sheets (31 strands; 128 residues). Acid phosphatase has three unique ligands consisting of a zinc ion (Zn), iron (III) ion (Fe) and a compound of N-Acetyl-D-glucosamine (C8H15NO6). The phosphatase enzyme requires these metal ions to catalyze reactions. So that in a reaction, the metal ion---such as a zinc ion--- influences the formation of a metal substrate complex.\

Medical Usage

Acid phosphatase is a peripheral membrane enzyme. When this enzyme is placed in a reversed micellar system the interaction of this enzyme with lipids resulted in the formation of complexes of lipoproteins (Kudryashova, E. V., et al.). Due to the results found in this reverse micellar matrix, they can be used in the medical field for diagnosis of diseases related to changes in lipid metabolism, as well as orthopedics and multiple others. Since lipids are crucial to the regulation of the body and its metabolism, the catalytic properties of acid phosphatase interacting with the membrane are largely dependent on the content of lipids along these membranes. Therefore, the catalytic behavior of acid phosphatases are regulated by the number of lipids along these membranes.

Sources/ References

Anklesaria, Jenifer H., et al. “Prostate Secretory Protein of 94 Amino Acids (PSP94) Binds to Prostatic Acid Phosphatase (PAP) in Human Seminal Plasma.” PLoS ONE, vol. 8, no. 3, Mar. 2013, pp. 1–10. EBSCOhost, doi:10.1371/journal.pone.0058631.

Kudryashova, E. V., et al. “Regulation of Catalytic Activity of Acid Phosphatase by Lipids in a Reverse Micellar System.” Biochemistry (00062979), vol. 74, no. 3, Mar. 2009, pp. 342–349. EBSCOhost, doi:10.1134/S0006297909030146.

Luciano, Carl S., and Sandra J. Newell. “Effects of Prey, Pitcher Age, and Microbes on Acid Phosphatase Activity in Fluid from Pitchers of Sarracenia Purpurea (Sarraceniaceae).” PLoS ONE, vol. 12, no. 7, July 2017, pp. 1–17. EBSCOhost, doi:10.1371/journal.pone.0181252.

Muniyan, Sakthivel, et al. “Human Prostatic Acid Phosphatase: Structure, Function and Regulation.” International Journal of Molecular Sciences, vol. 14, no. 5, May 2013, pp. 10438–10464. EBSCOhost, doi:10.3390/ijms140510438.

Pant, H. K. “Phosphatase.” AccessScience, McGraw-Hill Education, 2014.

The Protein Data Bank H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne (2000) Nucleic Acids Research, 28: 235-242. doi:10.1093/nar/28.1.235