Comments (originally from EcoCyc) Alkaline phosphatase catalyzes the hydrolysis of a wide variety of phosphomonoesters. The reaction proceeds through a phosphoseryl intermediate. The enzyme will also catalyze a transphosphorylation reaction with the transfer of the phosphoryl group to the alcohol in the presence of certain phosphate acceptors. Alkaline phosphatase is a metalloenzyme, binding two zinc atoms and one magnesium ion per monomer. The enzyme has been crystallized. 
- EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- Sowadski, JM et al. (1985) Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution. J. Mol. Biol. 186 417-33 PubMed
- Xu, X & Kantrowitz, ER (1991) A water-mediated salt link in the catalytic site of Escherichia coli alkaline phosphatase may influence activity. Biochemistry 30 7789-96 PubMed
- Janeway, CM et al. (1993) Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis. Biochemistry 32 1601-9 PubMed
- Coleman, JE (1992) Structure and mechanism of alkaline phosphatase. Annu Rev Biophys Biomol Struct 21 441-83 PubMed
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