Alkaline phosphatase

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{{STRUCTURE_1elx| PDB=1elx | SIZE=400| SCENE= |right|CAPTION=E. coli alkaline phosphatase dimer with Zn+2 (grey), Mg+2 (green) and phosphate ions, [[1elx]] }}
{{STRUCTURE_1elx| PDB=1elx | SIZE=400| SCENE= |right|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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'''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.
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== Disease ==
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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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== Structural highlights ==
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The ALP active site includes the Zn+2 and Mg+2 ions.
== 3D Structures of alkaline phosphatase ==
== 3D Structures of alkaline phosphatase ==
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**[[1k7h]] – nsALP + Zn + maleic acid – northern shrimp<br />
**[[1k7h]] – nsALP + Zn + maleic acid – northern shrimp<br />
**[[1shq]] - nsALP + Zn + Mg<br />
**[[1shq]] - nsALP + Zn + Mg<br />
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**[[1zeb]] - hALP + Zn + Mg – human<br />
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**[[1zeb]] - hALPP + Zn + Mg – human<br />
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**[[1zef]] - hALP + Zn + Mg + phenylalanine<br />
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**[[1zef]] - hALPP + Zn + Mg + phenylalanine<br />
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**[[2glq]] - hALP + Zn + Mg + Sr<br />
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**[[2glq]] - hALPP + Zn + Mg + Sr<br />
**[[3e2d]] – ALP + Zn + Mg – ''Vibrio''<br />
**[[3e2d]] – ALP + Zn + Mg – ''Vibrio''<br />
**[[3a52]] - ALP + Zn + Mg – ''Shewanella''<br />
**[[3a52]] - ALP + Zn + Mg – ''Shewanella''<br />
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**[[1ew9]] - EcALP + Zn + Mg + mercaptomethyl phosphonate<br />
**[[1ew9]] - EcALP + Zn + Mg + mercaptomethyl phosphonate<br />
**[[1shn]] - nsALP + Zn + phosphate<br />
**[[1shn]] - nsALP + Zn + phosphate<br />
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**[[1zed]] - hALP + Zn + Mg + PO3 + nitrophenyl hydrogen methylphosphonate<br />
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**[[1zed]] - hALPP + Zn + Mg + PO3 + nitrophenyl hydrogen methylphosphonate<br />
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**[[3mk0]], [[3mk1]] - hALP + Zn + Mg + phosphate + nitrophenol + phosphoserine<br />
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**[[3mk0]], [[3mk1]] - hALPP + Zn + Mg + phosphate + nitrophenol + phosphoserine<br />
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**[[3mk2]] - hALP + Zn + Mg + phosphoserine<br />
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**[[3mk2]] - hALPP + Zn + Mg + phosphoserine<br />
**[[2iuc]] - AbALP + Zn + Mg + phosphate – ''Antarctic bacterium''<br />
**[[2iuc]] - AbALP + Zn + Mg + phosphate – ''Antarctic bacterium''<br />
**[[2w5v]], [[2w5x]] - AbALP (mutant) + Zn + Mg + phosphoserine<br />
**[[2w5v]], [[2w5x]] - AbALP (mutant) + Zn + Mg + phosphoserine<br />

Revision as of 08:44, 29 October 2015

Template:STRUCTURE 1elx

Contents

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.

Disease

High levels of ALP are associated with hyperphosphatasia with mental retardation syndrome.

Relevance

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.

Structural highlights

The ALP active site includes the Zn+2 and Mg+2 ions.

3D Structures of alkaline phosphatase

Updated on 29-October-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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