Acid phosphatase (systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion
Acid phosphatase (EC 3.1.3.2, systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. It is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is present in many animal and plant species.
- Henneberry MO, Engel G, Grayhack JT (October 1979). “Acid phosphatase”. The Urologic Clinics of North America. 6 (3): 629–41. doi:10.1016/S0094-0143(21)01218-0. PMID 388794.
- Bull H, Murray PG, Thomas D, Fraser AM, Nelson PN (April 2002). “Acid phosphatases”. Molecular Pathology. 55 (2): 65–72. doi:10.1136/mp.55.2.65. PMC 1187150. PMID 11950951.
Different forms of acid phosphatase are found in different organs, and their serum levels are used to evaluate the success of the surgical treatment of prostate cancer. In the past, they were also used to diagnose this type of cancer.
- Henneberry MO, Engel G, Grayhack JT (October 1979). “Acid phosphatase”. The Urologic Clinics of North America. 6 (3): 629–41. doi:10.1016/S0094-0143(21)01218-0. PMID 388794.Bull H, Murray PG, Thomas D, Fraser AM, Nelson PN (April 2002). “Acid phosphatases”. Molecular Pathology. 55 (2): 65–72. doi:10.1136/mp.55.2.65. PMC 1187150. PMID 11950951.
It’s also used as a cytogenetic marker to distinguish the two different lineages of acute lymphoblastic leukemia (ALL) : B-ALL (a leukemia of B lymphocytes) is acid-phosphatase negative , T-ALL (originating instead from T Lymphocytes) is acid-phosphatase positive .
Acid phosphatase catalyzes the following reaction at an optimal acidic pH (below 7):a phosphate monoester + H2O = an alcohol + phosphate
Phosphatase enzymes are also used by soil microorganisms to access organically bound phosphate nutrients. An assay on the rates of activity of these enzymes may be used to ascertain biological demand for phosphates in the soil.
Some plant roots, especially cluster roots, exude carboxylates that perform acid phosphatase activity, helping to mobilise phosphorus in nutrient-deficient soils.
Certain bacteria, such as Nocardia, can degrade this enzyme and utilize it as a carbon source.
Bone acid phosphatase
Tartrate-resistant acid phosphatase may be used as a biochemical marker of osteoclast function during the process of bone resorption.
- Minkin C (May 1982). “Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function”. Calcified Tissue International. 34 (3): 285–90. doi:10.1007/BF02411252. PMID 6809291. S2CID 22706943.
Genes
The following genes encode the polypeptide components for various acid phosphatase isoenzymes:[citation needed]
- ACP1
- ACP2
- ACPP (ACP3), prostatic acid phosphatase
- ACP5, tartrate-resistant acid phosphatase
- ACP6
- ACPT, testicular acid phosphatase
- Tissue acid phosphatase, or lysosomal acid phosphatase
Gold sodium thiomalate
Sodium aurothiomalate (INN, known in the United States as gold sodium thiomalate) is a gold compound that is used for its immunosuppressive anti-rheumatic effects. Along with an orally-administered gold salt, auranofin, it is one of only two gold compounds currently employed in modern medicine. Its precise mechanism of action is unknown but is known that it inhibits the synthesis of prostaglandins. It also modulates phagocytic cells and inhibits class II major histocompatibility complex-peptide interactions. It is also known that it inhibits the following enzymes:
- Acid phosphatase
- Beta-glucuronidase
- Elastase
- Cathepsin G
- Thrombin
- Microsomal prostaglandin E synthase-1
- Jessop JD, O’Sullivan MM, Lewis PA, Williams LA, Camilleri JP, Plant MJ, Coles EC (September 1998). “A long-term five-year randomized controlled trial of hydroxychloroquine, sodium aurothiomalate, auranofin and penicillamine in the treatment of patients with rheumatoid arthritis”. British Journal of Rheumatology. 37 (9): 992–1002. doi:10.1093/rheumatology/37.9.992. PMID 9783766.
- Iqbal MS, Saeed M, Taqi SG (2008). “Erythrocyte membrane gold levels after treatment with auranofin and sodium aurothiomalate”. Biological Trace Element Research. 126 (1–3): 56–64. doi:10.1007/s12011-008-8184-x. PMID 18649049. S2CID 20169992.
- Kean WF, Kean IR (June 2008). “Clinical pharmacology of gold”. Inflammopharmacology. 16 (3): 112–25. doi:10.1007/s10787-007-0021-x. PMID 18523733. S2CID 808858.
- Berners-Price SJ, Filipovska A (September 2011). “Gold compounds as therapeutic agents for human diseases”. Metallomics. 3 (9): 863–73. doi:10.1039/c1mt00062d. PMID 21755088.
- Tuure L, Hämäläinen M, Moilanen T, Moilanen E (2014). “Aurothiomalate inhibits the expression of mPGES-1 in primary human chondrocytes”. Scandinavian Journal of Rheumatology. 44 (1): 74–9. doi:10.3109/03009742.2014.927917. PMID 25314295. S2CID 5213201.
See also
References
- Henneberry MO, Engel G, Grayhack JT (October 1979). “Acid phosphatase”. The Urologic Clinics of North America. 6 (3): 629–41. doi:10.1016/S0094-0143(21)01218-0. PMID 388794.
- Bull H, Murray PG, Thomas D, Fraser AM, Nelson PN (April 2002). “Acid phosphatases”. Molecular Pathology. 55 (2): 65–72. doi:10.1136/mp.55.2.65. PMC 1187150. PMID 11950951.
- Minkin C (May 1982). “Bone acid phosphatase: tartrate-resistant acid phosphatase as a marker of osteoclast function”. Calcified Tissue International. 34 (3): 285–90. doi:10.1007/BF02411252. PMID 6809291. S2CID 22706943.
External links
- Acid+phosphatase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.3.2
