Alkaline phosphatase
FunctionAlkaline 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) DiseaseHigh levels of ALP are associated with hyperphosphatasia with mental retardation syndrome. RelevanceALP 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 highlightsThe .[2] Water molecules are shown as red spheres.
3D Structures of alkaline phosphataseAlkaline phosphatase 3D structures
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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