World Library  
Flag as Inappropriate
Email this Article

Acid phosphatase

Article Id: WHEBN0004876457
Reproduction Date:

Title: Acid phosphatase  
Author: World Heritage Encyclopedia
Language: English
Subject: Prostatic acid phosphatase, R.EcoRII, EC, Biochemistry, Pre-ejaculate
Collection: Biochemistry, Ec
Publisher: World Heritage Encyclopedia

Acid phosphatase

Acid phosphatase
EC number
CAS number 9001-77-8
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Acid phosphatase (EC, acid phosphomonoesterase, phosphomonoesterase, glycerophosphatase, acid monophosphatase, acid phosphohydrolase, acid phosphomonoester hydrolase, uteroferrin, acid nucleoside diphosphate phosphatase, orthophosphoric-monoester phosphohydrolase (acid optimum)) is a phosphatase, a type of enzyme, used to free attached phosphoryl groups from other molecules during digestion. It can be further classified as a phosphomonoesterase. Acid phosphatase is stored in lysosomes and functions when these fuse with endosomes, which are acidified while they function; therefore, it has an acid pH optimum.[1] This enzyme is present in many animal and plant species.[2]

Different forms of acid phosphatase are found in different serum levels are used to evaluate the success of the surgical treatment of prostate cancer.[1] In the past, they were also used to diagnose this type of cancer.

Reference ranges for blood tests, showing acid phosphatase in red at left.

Acid phosphatase catalyzes the following reaction at an optimal acidic pH (below 7):

Orthophosphoric monoester + H2O → alcohol + H3PO4

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 like Nocardia, can degrade this enzyme and utilize it as a carbon source


  • Bone acid phosphatase 1
  • Genes 2
  • References 3
  • See also 4
    • Internal links 4.1
  • External links 5

Bone acid phosphatase

Tartrate-resistant acid phosphatase may be used as a biochemical marker of osteoclast function during the process of bone resorption.[3]


The following genes encode the polypeptide components for various acid phosphatase isoenzymes.


  1. ^ a b Henneberry, M.O.; Engel, G.; Grayhack, J.T. (October 1979). "Acid phosphatase". The Urologic clinics of North America 6 (3): 629–41. Retrieved 11 May 2015. 
  2. ^ Bull, H.; Murray, P.G.; Thomas, D.; Fraser, A.M.; Nelson, P.N. (April 2002). "Acid phosphatases". Molecular Pathology 55 (2): 65–72. Retrieved 11 May 2015. 
  3. ^ Minkin, Cedrick (1982). "Bone Acid Phosphatase: Tartrate-resistant Acid Phosphatase as a Marker of Osteoclast Function". Calcified Tissue International 34: 285–290. Retrieved 11 May 2015. 

See also

Internal links

External links

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Project Gutenberg are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.