InterPro domain: IPR017850

This superfamily represents a structural domain with a core 3-layer alpha/beta/alpha structure, which can sometimes contain additional subdomains (also covered by this entry). These domains form the core domain of alkaline phosphatases. This structural domain is found in:

• Alkaline phosphatase ( 3.1.3.1 ); most use zinc and magnesium as cofactors [ 1 , 2 ].
• Arylsulphatase (has an additional C-terminal alpha+beta subdomain) ( 3.1.6.8 ) [ 3 , 4 ].
• Phosphoglycerate mutase (catalytic domain) ( 5.4.2.1 ) [ 5 ].
• Phosphonoacetate hydrolase (contains an alpha+beta subdomain inserted near C terminus) ( 3.11.1.2 ); uses zinc as a cofactor.
• Phosphoenolmutase ( 5.4.2.7 ).

1. Metal specificity is correlated with two crucial active site residues in Escherichia coli alkaline phosphatase. Biochemistry 44, 8378-86
2. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J. Mol. Biol. 350, 441-51
3. Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry 37, 3654-64
4. Structure of human estrone sulfatase suggests functional roles of membrane association. J. Biol. Chem. 278, 22989-97
5. Insights into the catalytic mechanism of cofactor-independent phosphoglycerate mutase from X-ray crystallography, simulated dynamics and molecular modeling. J. Mol. Biol. 328, 909-20