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Acid phosphatase (EC 3.1.3.2, acid phosphomonoesterase', phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid phosphohydrolase, acid phosphomonoester hydrolase, uteroferrin, acid nucleoside diphosphate phosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum), systematic name phosphate-monoester phosphohydrolase (acid optimum)) is an enzyme that frees attached phosphoryl groups from other molecules during
digestion Digestion is the breakdown of large insoluble food molecules into small water-soluble food molecules so that they can be absorbed into the watery blood plasma. In certain organisms, these smaller substances are absorbed through the small intest ...
. It can be further classified as a phosphomonoesterase. It is stored in
lysosome A lysosome () is a membrane-bound organelle found in many animal cells. They are spherical vesicles that contain hydrolytic enzymes that can break down many kinds of biomolecules. A lysosome has a specific composition, of both its membrane p ...
s and functions when these fuse with
endosome Endosomes are a collection of intracellular sorting organelles in eukaryotic cells. They are parts of endocytic membrane transport pathway originating from the trans Golgi network. Molecules or ligands internalized from the plasma membrane can ...
s, which are acidified while they function; therefore, it has an acid pH optimum. This enzyme is present in many animal and plant species. Different forms of acid phosphatase are found in different
organ Organ may refer to: Biology * Organ (biology), a part of an organism Musical instruments * Organ (music), a family of keyboard musical instruments characterized by sustained tone ** Electronic organ, an electronic keyboard instrument ** Hammond ...
s, and their
serum Serum may refer to: * Serum (blood), plasma from which the clotting proteins have been removed **Antiserum, blood serum with specific antibodies for passive immunity * Serous fluid, any clear bodily fluid *Truth serum, a drug that is likely to mak ...
levels are used to evaluate the success of the surgical treatment of
prostate cancer Prostate cancer is cancer of the prostate. Prostate cancer is the second most common cancerous tumor worldwide and is the fifth leading cause of cancer-related mortality among men. The prostate is a gland in the male reproductive system that su ...
. In the past, they were also used to diagnose this type of cancer. 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 root Cluster roots, also known as proteoid roots, are plant roots that form clusters of closely spaced short lateral rootlets. They may form a two- to five-centimetre-thick mat just beneath the leaf litter. They enhance nutrient uptake, possibly by chem ...
s, exude
carboxylate In organic chemistry, a carboxylate is the conjugate base of a carboxylic acid, (or ). It is an ion with negative charge. Carboxylate salts are salts that have the general formula , where M is a metal and ''n'' is 1, 2,...; ''carboxylat ...
s that perform acid phosphatase activity, helping to mobilise
phosphorus Phosphorus is a chemical element with the symbol P and atomic number 15. Elemental phosphorus exists in two major forms, white phosphorus and red phosphorus, but because it is highly reactive, phosphorus is never found as a free element on Ea ...
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 Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic iso ...
may be used as a biochemical marker of
osteoclast An osteoclast () is a type of bone cell that breaks down bone tissue. This function is critical in the maintenance, repair, and remodeling of bones of the vertebral skeleton. The osteoclast disassembles and digests the composite of hydrated pro ...
function during the process of
bone resorption Bone resorption is resorption of bone tissue, that is, the process by which osteoclasts break down the tissue in bones and release the minerals, resulting in a transfer of calcium from bone tissue to the blood. The osteoclasts are multi-nuclea ...
.


Genes

The following genes encode the polypeptide components for various acid phosphatase isoenzymes. * ACP1 *
ACP2 Lysosomal acid phosphatase is an enzyme that in humans is encoded by the ''ACP2'' gene. Lysosomal acid phosphatase is composed of two subunits, alpha and beta, and is chemically and genetically distinct from red cell acid phosphatase. Lysosomal ...
* ACPP ( ACP3), Prostatic acid phosphatase * ACP5,
Tartrate-resistant acid phosphatase Tartrate-resistant acid phosphatase (TRAP or TRAPase), also called acid phosphatase 5, tartrate resistant (ACP5), is a glycosylated monomeric metalloprotein enzyme expressed in mammals. It has a molecular weight of approximately 35kDa, a basic iso ...
* ACP6 * ACPT, Testicular acid phosphatase * Tissue acid phosphatase, or Lysosomal acid phosphatase


See also

*
Alkaline phosphatase The enzyme alkaline phosphatase (EC 3.1.3.1, alkaline phosphomonoesterase; phosphomonoesterase; glycerophosphatase; alkaline phosphohydrolase; alkaline phenyl phosphatase; orthophosphoric-monoester phosphohydrolase (alkaline optimum), systematic ...


References


External links

* * {{DEFAULTSORT:Acid Phosphatase EC 3.1.3.2 Biochemistry