Alkaline phosphatase

Function

Alkaline phosphatase (ALP) is an enzyme which removes phosphate from nucleotides, proteins and alkaloids. The enzyme is most effective in alkaline environment. Human ALP is present as 3 tissue-associated isozymes: intestinal, tissue-nonspecific and placental (ALPP). ALP is a zinc and magnesium containing enzyme. ALP is a glycoprotein which is attached by a GPI anchor to cell surfaces.^[1]

See Alkaline phosphatase (Hebrew)

Disease

High levels of ALP are associated with hyperphosphatasia with mental retardation syndrome.

Relevance

ALP is used in molecular biology to remove the phosphate at the 5' end of DNA thus preventing its self ligation. ALP activity is used in the dairy industry as a marker for successful pasteurization since it does not denature at temperatures which kill bacteria in milk.

Structural highlights

The .^[2] Water molecules are shown as red spheres.

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3D Structures of alkaline phosphatase

Alkaline phosphatase 3D structures

E. coli alkaline phosphatase dimer with Zn+2 (grey), Mg+2 (green) and phosphate ions, 1elx

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:15946677 doi:http://dx.doi.org/10.1016/j.jmb.2005.04.068
↑ Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER. Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102. J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:9533886 doi:10.1006/jmbi.1998.1635

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

[1] Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:15946677 doi:http://dx.doi.org/10.1016/j.jmb.2005.04.068

[2] Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER. Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102. J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:9533886 doi:10.1006/jmbi.1998.1635

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