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Alkaline phosphatase
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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.<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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== 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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| - | **[[1khl]], [[3dyc]], [[4km4]] - EcALP (mutant) + Zn + phosphate<br /> | ||
| - | **[[1alh]], [[3tg0]] - EcALP + Zn + phosphate<br /> | ||
| - | **[[1y6v]] - EcALP + Co + phosphate<br /> | ||
| - | **[[1y7a]] - EcALP (mutant) + Co + phosphate<br /> | ||
| - | **[[1elx]], [[1ely]], [[1elz]], [[1kh9]], [[1kh4]], [[2g9y]], [[3cmr]] - EcALP (mutant) + Zn + Mg + phosphate<br /> | ||
| - | **[[3dpc]] - EcALP (mutant) + phosphorylated peptide<br /> | ||
| - | **[[2ga3]] - EcALP (mutant) + Zn + Mg + phosphothreonine<br /> | ||
| - | **[[1ew8]] - EcALP + Zn + phosphonoacetic acid + phosphate<br /> | ||
| - | **[[1ew9]] - EcALP + Zn + Mg + mercaptomethyl phosphonate<br /> | ||
| - | **[[1shn]] - nsALP + Zn + phosphate<br /> | ||
| - | **[[1zed]] - hALPP + Zn + Mg + PO3 + nitrophenyl hydrogen methylphosphonate<br /> | ||
| - | **[[3mk0]], [[3mk1]] - hALPP + Zn + Mg + phosphate + nitrophenol + phosphoserine<br /> | ||
| - | **[[3mk2]] - hALPP + Zn + Mg + phosphoserine<br /> | ||
| - | **[[2iuc]] - AbALP + Zn + Mg + phosphate – ''Antarctic bacterium''<br /> | ||
| - | **[[2w5v]], [[2w5x]] - AbALP (mutant) + Zn + Mg + phosphoserine<br /> | ||
| - | **[[2w5w]] - AbALP (mutant) + Zn + phosphoserine<br /> | ||
| - | **[[2x98]] - ALP + Zn + Mg + phosphate – ''Halobacterium salinarum''<br /> | ||
| - | **[[4a9x]] - PfALP Phox + Fe2O + Ca + A[β,γ-methylene]TP <br /> | ||
| - | **[[4alf]] - PfALP Phox + Fe2O + Ca + phosphate <br /> | ||
| - | **[[4kjd]] - rALP + Mg + phosphoserine – rat<br /> | ||
| - | **[[4kjg]] - rALP + Zn + Mg + nitrophenyl phosphate <br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[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
