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Alkaline phosphatase

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{{STRUCTURE_1elx| PDB=1elx | SIZE=400| SCENE= |right|CAPTION=E. coli alkaline phosphatase dimer with Zn+2, Mg+2 and phosphate ions, [[1elx]] }}
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<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]]'>
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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.
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== Function ==
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'''Fructose bisphosphate aldolase''' is an enzyme in glycolysis and gluconeogenesis. Glycolyis is responsible for the conversion of glucose into two three-carbon pyruvate molecules without the need for oxygen. The process generates two net ATP. The overall reaction is:
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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>
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Glucose + 2 NAD+ + 2 ADP + 2 Pi --> 2 pyruvate (3-carbon product) + 2 NADH + 2 ATP + 2 H20 + 4 H+
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See [[Alkaline phosphatase (Hebrew)]]
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Gluconeogenesis is responsible for maintaining the appropriate levels of blood glucose in animals by generating glucose from non-carbohydrate precursors. Gluconeogenesis can make glucose from lactate, pyruvate, citric acid cycle intermediates and from most amino acids (the exceptions being leucine and lysine). The common intermediate for all of the precursors on their way to becoming glucose must be oxaloacetate.
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== Disease ==
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The aldolase catalyzes the reversible cleavage of fructose-1,6-bisphosphate into dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (GAP). Different isozymes of aldolase can also catalyze the cleavage of fructose 1-phosphate to diydroxyacetone and glyceraldehyde (GA). Different isozymes exhibit preferences for either or both of the substrates, depending on the role of the aldolase (i.e. gluconeogenesis versus glycolysis).<ref name="book">Voet, D, Voet, J, & Pratt, C. (2008). Fundamentals of biochemistry, third edition. Hoboken, NJ: Wiley & Sons, Inc.</ref>
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High levels of ALP are associated with hyperphosphatasia with mental retardation syndrome.
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== Relevance ==
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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.
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== 3D Structures of alkaline phosphatase ==
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== Structural highlights ==
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''Update November 2011''
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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.
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*<scene name='47/471754/Cv/4'>Zn cluster</scene>.
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*<scene name='47/471754/Cv/5'>Mg+2 coordination site</scene>.
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[[1alk]], [[1ed9]], [[1ed8]] – EcALP + Zn + Mg – ''Eschechia coli''<br />
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== 3D Structures of alkaline phosphatase ==
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[[3bdh]] - EcALP + Mg<br />
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[[Alkaline phosphatase 3D structures]]
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[[1aja]], [[3bdf]], [[3bdg]] – EcALP (mutant) <br />
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[[1ali]], [[1ajb]], [[1ajc]], [[1ajd]], [[1alj]], [[1ani]], [[1anj]], [[2anh]], [[1hqa]], [[1urb]], [[1hjk]], [[1khk]], [[1kh7]] - EcALP (mutant) + Zn + Mg<br />
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[[1ura]] - EcALP (mutant) + Zn<br />
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[[1khn]] - EcALP (mutant) + Zn<br />
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[[1b8j]] - EcALP + Zn + Mg + VO4<br />
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[[1kh5]] - EcALP (mutant) + Zn + Mg + AlF3<BR />
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[[1khj]] - EcALP (mutant) + Zn + AlF3<BR />
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[[1k7h]] – nsALP + Zn + maleic acid – northern shrimp<br />
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[[1shq]] - nsALP + Zn + Mg<br />
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[[1zeb]] - hALP + Zn + Mg – human<br />
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[[1zef]] - hALP + Zn + Mg + phenylalanine<br />
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[[2glq]] - hALP + Zn + Mg + Sr<br />
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[[3e2d]] – ALP + Zn + Mg – ''Vibrio''<br />
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[[3a52]] - ALP + Zn + Mg – ''Shewanella''
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===ALP complexes with phosphate derivative===
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[[1khl]], [[3dyc]] - EcALP (mutant) + Zn + phosphate<br />
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</StructureSection>
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[[1alh]], [[3tg0]] - EcALP + Zn + phosphate<br />
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[[1y6v]] - EcALP + Co + phosphate<br />
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[[1y7a]] - EcALP (mutant) + Co + phosphate<br />
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[[1elx]], [[1ely]], [[1elz]], [[1kh9]], [[1kh4]], [[2g9y]], [[3cmr]] - EcALP (mutant) + Zn + Mg + phosphate<br />
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[[3dpc]] - EcALP (mutant) + phosphorylated peptide<br />
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[[2ga3]] - EcALP (mutant) + Zn + Mg + phosphothreonine<br />
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[[1ew8]] - EcALP + Zn + phosphonoacetic acid + phosphate<br />
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[[1ew9]] - EcALP + Zn + Mg + mercaptomethyl phosphonate<br />
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[[1shn]] - nsALP + Zn + phosphate<br />
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[[1zed]] - hALP + Zn + Mg + PO3 + nitrophenyl hydrogen methylphosphonate<br />
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[[3mk0]], [[3mk1]] - hALP + Zn + Mg + phosphate + nitrophenol + phosphoserine<br />
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[[3mk2]] - hALP + Zn + Mg + phosphoserine<br />
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[[2iuc]] - AbALP + Zn + Mg + phosphate – Antarctic bacterium<br />
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[[2w5v]], [[2w5x]] - AbALP (mutant) + Zn + Mg + phosphoserine<br />
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[[2w5w]] - AbALP (mutant) + Zn + phosphoserine<br />
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[[2x98]] - ALP + Zn + Mg + phosphate – ''Halobacterium salinarum''
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

References

  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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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