Alkaline phosphatase
From Proteopedia
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'''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> | '''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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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. | 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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| - | **[[2mlx]], [[2mly]], [[2mlz]] - EcALP residues 220-310 + trigger factor - NMR<br /> | ||
| - | **[[5jtl]] – EcALP + SecB<br /> | ||
| - | **[[5too]] - EmALP (mutant) + Zn <br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
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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
