Alkaline phosphatase
From Proteopedia
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| - | <StructureSection load='1elx' size=' | + | <StructureSection load='1elx' size='400' side='right' scene='47/471754/Cv/1' caption='E. coli alkaline phosphatase dimer with Zn+2 (grey), Mg+2 (green) and phosphate ions, [[1elx]]'> | 
| == Function == | == 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. | + | '''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.<ref>PMID:15946677</ref> | 
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| + | See [[Alkaline phosphatase (Hebrew)]] | ||
| == Disease == | == Disease == | ||
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| == Structural highlights == | == Structural highlights == | ||
| - | The <scene name='47/471754/Cv/ | + | The <scene name='47/471754/Cv/3'>ALP active site includes the Zn+2 and Mg+2 ions</scene>.<ref>PMID:9533886</ref> Water molecules are shown as red spheres. | 
| - | </ | + | *<scene name='47/471754/Cv/4'>Zn cluster</scene>. | 
| + | *<scene name='47/471754/Cv/5'>Mg+2 coordination site</scene>. | ||
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| == 3D Structures of alkaline phosphatase == | == 3D Structures of alkaline phosphatase == | ||
| + | [[Alkaline phosphatase 3D structures]] | ||
| - | + | </StructureSection> | |
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| - | + | == References == | |
| - | + | <references/> | |
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| [[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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References
- ↑ 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
